|
Name |
Accession |
Description |
Interval |
E-value |
| NOS_oxygenase_euk |
cd00795 |
Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by ... |
1-380 |
0e+00 |
|
Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain, which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOS's also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN.
Pssm-ID: 238410 Cd Length: 412 Bit Score: 872.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 1 MGSIMHPSQHARRPEDVRTKGQLFPLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRN 80
Cdd:cd00795 33 LGSIMDPKKLTRRPRDGRPKEELLPQAKDFINQYYSSIKRSGSEAHLARLEEVTKEIEATGTYQLTEDELIFGAKQAWRN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 81 ASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGS 160
Cdd:cd00795 113 APRCIGRIQWSKLQVFDARDCTTAQEMFEAICNHIKYATNKGNLRSAITVFPQRTDGKHDFRIWNSQLIRYAGYKQPDGS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 161 TLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNML 240
Cdd:cd00795 193 IIGDPANVEFTELCIKLGWKPKYGRFDVLPLVLQANGEDPELFEIPPELVLEVPIEHPKYEWFKELGLKWYALPAVSNML 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 241 LEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDH 320
Cdd:cd00795 273 LEIGGLEFTACPFNGWYMGTEIGVRDLCDQQRYNILEEVAKKMGLDTRKTSSLWKDKALVEINVAVLHSFQKANVTIVDH 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 321 HSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPW 380
Cdd:cd00795 353 HSASESFMKHMENEYRARGGCPADWVWIVPPMSGSITPVFHQEMLNYVLSPSYEYQPDPW 412
|
|
| Nitric_oxide_synthase |
cd06202 |
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ... |
665-1068 |
0e+00 |
|
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses with a heme-containing N-terminal oxidase domain. The reductase portion is similar in structure to NADPH dependent cytochrome-450 reductase (CYPOR), having an inserted connecting sub-domain within the FAD binding portion of FNR. NOS differs from CYPOR in a requirement for the cofactor tetrahydrobiopterin and unlike most CYPOR is dimeric. Nitric oxide synthase produces nitric oxide in the conversion of L-arginine to L-citruline. NOS has been implicated in a variety of processes including cytotoxicity, anti-inflamation, neurotransmission, and vascular smooth muscle relaxation.
Pssm-ID: 99799 [Multi-domain] Cd Length: 406 Bit Score: 777.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 665 RLLSRQNLQSPKSSRSTIFVRLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGV 744
Cdd:cd06202 1 KVISRQNLQSPKSSRSTILVKLDTNGAQELHYQPGDHVGIFPANRPELVDALLDRLHDAPPPDQVIKLEVLEERSTALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 745 ISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEYEEWKWGKNPTIVEVLEEFPS 824
Cdd:cd06202 81 IKTWTPHERLPPCTLRQALTRYLDITTPPTPQLLQLLATLATDEKDKERLEVLGKGSSEYEDWKWYKNPNILEVLEEFPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 825 IQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFH 904
Cdd:cd06202 161 LQVPASLLLTQLPLLQPRYYSISSSPDMYPGEIHLTVAVVSYRTRDGQGPVHHGVCSTWLNGLTPGDTVPCFVRSAPSFH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 905 LPRNPQVPCILVGPGTGIAPFRSFWQQRQFDI---QHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAY 981
Cdd:cd06202 241 LPEDPSVPVIMVGPGTGIAPFRSFWQQRQYDLrmsEDPGKKFGDMTLFFGCRNSTIDDIYKEETEEAKNKGVLTEVYTAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 982 SREPDKPKKYVQDILQEQlAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRYHE 1061
Cdd:cd06202 321 SREPGKPKTYVQDLLKEQ-AESVYDALVREGGHIYVCGDVTMAEDVSQTIQRILAEHGNMSAEEAEEFILKLRDENRYHE 399
|
....*..
gi 323635434 1062 DIFGVTL 1068
Cdd:cd06202 400 DIFGVTL 406
|
|
| NO_synthase |
pfam02898 |
Nitric oxide synthase, oxygenase domain; |
19-380 |
0e+00 |
|
Nitric oxide synthase, oxygenase domain;
Pssm-ID: 460742 Cd Length: 362 Bit Score: 767.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 19 TKGQLFPLAKEFIDQYYSSIKRFgSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDA 98
Cdd:pfam02898 1 PKEELLEEAKEFIEQYYTELKRS-SEEHEARWEEVRAEIEETGTYQHTYEELAYGAKLAWRNSNRCIGRIFWSKLQVFDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 99 RDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQG 178
Cdd:pfam02898 80 RHVTTEEEMFEALCNHIKYATNGGNIRSAITIFPPRTDGKHDFRIWNHQLIRYAGYEQPDGSVIGDPANVEFTELCEKLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 179 WKPPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYM 258
Cdd:pfam02898 160 WKGKGTRFDVLPLVIQANGEDPKLFEIPPELVLEVPIEHPEYEWFAELGLKWYAVPAISNMRLEIGGIEYTAAPFNGWYM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 259 GTEIGVRDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCR 338
Cdd:pfam02898 240 GTEIGARNLADEYRYNLLEKVAKKMGLDTRSNSSLWKDRALVELNVAVLHSFQKAGVTIVDHHTAAEQFMKHEENEQRAG 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 323635434 339 GGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPW 380
Cdd:pfam02898 320 RGCPGDWVWLVPPLSGSTTPVFHQEMDNYILKPNFFYQEDPW 361
|
|
| COG4362 |
COG4362 |
Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism]; |
27-378 |
0e+00 |
|
Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism];
Pssm-ID: 443495 Cd Length: 360 Bit Score: 576.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 27 AKEFIDQYYSSIKRFGSkAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHG 106
Cdd:COG4362 10 AEEFLRQCYKELGKSEE-EVERRLAEVRAEIAATGTYTHTYEELEYGARVAWRNSNRCIGRLFWRSLQVRDRRHVTTPEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 107 MFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRF 186
Cdd:COG4362 89 VFEALVEHLRFATNGGKIRPTITVFAPDQPGRPGVRIWNHQLIRYAGYETEDGSVLGDPASVEFTDACQRLGWRGPRTAF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 187 DVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRD 266
Cdd:COG4362 169 DVLPLVIQVGGEPPRLFEIPRDLVLEVPITHPEYPWFAELGLRWYAVPAISNMRLEIGGIDYPAAPFNGWYMGTEIGARN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 267 YCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWV 346
Cdd:COG4362 249 LADEDRYNLLPKVAERMGLDTSSNRTLWKDRALVELNIAVLHSFKKAGVTIVDHHTASQQFLTFEQREEKAGREVTGDWS 328
|
330 340 350
....*....|....*....|....*....|..
gi 323635434 347 WIVPPMSGSITPVFHQEMLNYRLTPSFEYQPD 378
Cdd:COG4362 329 WLIPPMSGATTHVFHRYYDNEILKPNFFYQDD 360
|
|
| CysJ |
COG0369 |
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ... |
416-1064 |
1.83e-152 |
|
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440138 [Multi-domain] Cd Length: 561 Bit Score: 466.16 E-value: 1.83e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 416 QAMAKRVKATILYATETGKSQAYAKTLCEIFKHA-FDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCAL 494
Cdd:COG0369 21 AAAAAGTPLTILYGSQTGNAEGLAEQLAERAKAAgLAVTLASLDDYKPKDLAKEGLLLIVTSTYGEGEPPDNARAFYEFL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 495 MEMRhpnsvqeerksykvrfnsvssysdsqkssgdgpdlrdnfesAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEE 574
Cdd:COG0369 101 HSKK-----------------------------------------APKLDGLRYAVLGLGDSSYETFCQTGKDFDARLEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 575 LGGERILKMREGDElcGQEEAFRTWAKKVFKAACDVFcvgddvnieKANNSLISNDrswkrnkfrltfVAEAPELTqgls 654
Cdd:COG0369 140 LGATRLLPRVDCDV--DYEEAAEAWLAAVLAALAEAL---------GAAAAAAAAA------------AAAAPAYS---- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 655 nvhKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGSqELQYQPGDHLGVFPGNHEDLVNALIERLEDAPpvNQMVKVEl 734
Cdd:COG0369 193 ---RKNPFPATVLENRELTGRGSAKETRHIEIDLPGS-GLSYEPGDALGVWPENDPALVDELLARLGLDG--DEPVTLD- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 735 leerntalgvisnwtDElrlpPCTIFQAFKYYLDITTPPTPLqLQQFASLATSEKEKQrlLVLSKGLQEYEEWKWGKnpT 814
Cdd:COG0369 266 ---------------GE----PLSLREALTEHLELTRLTPPL-LEKYAELTGNAELAA--LLADEDKAALREYLAGR--Q 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 815 IVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTrdgEGPIHHGVCSSWLNRIQADELVP 894
Cdd:COG0369 322 LLDLLREFPAAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLTVGVVRYEA---SGRERKGVASTYLADLEEGDTVP 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 895 CFVRGAPSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDiQHKGMNpcpmVLVFGCRQSKIDHIYREETLQAKNKGVF 974
Cdd:COG0369 399 VFVEPNPNFRLPADPDTPIIMIGPGTGIAPFRAFLQEREAR-GASGKN----WLFFGDRHFTTDFLYQTELQAWLKDGVL 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 975 RELYTAYSREpDKPKKYVQDILQEQLAEsVYRALkEQGGHIYVCGDVT-MAADVLKAIQRIMTQQGKLSAEDAGVFISRM 1053
Cdd:COG0369 474 TRLDLAFSRD-QAEKIYVQHRLLEQGAE-LWAWL-EEGAHVYVCGDASrMAKDVDAALLDIIAEHGGLSEEEAEEYLAEL 550
|
650
....*....|.
gi 323635434 1054 RDDNRYHEDIF 1064
Cdd:COG0369 551 RAEKRYQRDVY 561
|
|
| FAD_binding_1 |
pfam00667 |
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ... |
655-883 |
4.56e-96 |
|
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, Nitric oxide synthase and methionine synthase reductase.
Pssm-ID: 395540 [Multi-domain] Cd Length: 219 Bit Score: 304.26 E-value: 4.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 655 NVHKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGSqELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVEL 734
Cdd:pfam00667 1 PFDAKKPFTAPVLSNRELTSPSSDRNCIHVELDISGS-GLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 735 LEErntalgvisnWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLS--KGLQEYEEWKWGKN 812
Cdd:pfam00667 80 LDE----------RVKPPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSsdAGAREYKRWKLNHA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323635434 813 PTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTrDGEGPIHHGVCSSW 883
Cdd:pfam00667 150 PTLLEVLEEFPSVKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEYET-DGEGRIHYGVCSNW 219
|
|
| cysJ |
TIGR01931 |
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an ... |
425-1064 |
1.30e-87 |
|
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an NADPH-dependent sulfite reductase flavoprotein subunit. Most members of this family are found in Cys biosynthesis gene clusters. The closest homologs below the trusted cutoff are designated as subunits nitrate reductase.
Pssm-ID: 273882 [Multi-domain] Cd Length: 597 Bit Score: 294.68 E-value: 1.30e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 425 TILYATETGKSQAYAKTLCEIFKHA-FDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNsv 503
Cdd:TIGR01931 62 TILYGSQTGNARRLAKRLAEKLEAAgFSVRLSSADDYKFKQLKKERLLLLVISTQGEGEPPEEAISLHKFLHSKKAPK-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 504 qeerksykvrfnsvssysdsqkssgdgpdlrdnfesagpLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKM 583
Cdd:TIGR01931 140 ---------------------------------------LENLRYSVLGLGDSSYEFFCQTGKDFDKRLEELGGKRLLPR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 584 REGDelCGQEEAFRTWAKKVFKAACDVFCVG-DDVNIEKANNSLISNDRSW-KRNKFRltfvaeapeltqglsnvhkkrv 661
Cdd:TIGR01931 181 VDAD--LDYDANAAEWRAGVLTALNEQAKGGaSTPSASETSTPLQTSTSVYsKQNPFR---------------------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 662 saARLLSRQNLQSPKSSRSTIFVRLHTNGSqELQYQPGDHLGVFPGNHEDLVNALIERLEDAPpvNQMVKVElleernta 741
Cdd:TIGR01931 237 --AEVLENQKITGRNSKKDVRHIEIDLEGS-GLHYEPGDALGVWYKNDPALVKEILKLLNLDP--DEKVTIG-------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 742 lgvisnwtDELRlppcTIFQAFKYYLDITTPPTPLqLQQFASLATSEkEKQRLLVLSKGLQEYEEwkwgkNPTIVEVLEE 821
Cdd:TIGR01931 304 --------GKTI----PLFEALITHFELTQNTKPL-LKAYAELTGNK-ELKALIADNEKLKAYIQ-----NTPLIDLIRD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 822 FPSiQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYrtrDGEGPIHHGVCSSWL-NRIQADELVPCFVRGA 900
Cdd:TIGR01931 365 YPA-DLDAEQLISLLRPLTPRLYSISSSQSEVGDEVHLTVGVVRY---QAHGRARLGGASGFLaERLKEGDTVPVYIEPN 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 901 PSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQfDIQHKGMNpcpmVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTA 980
Cdd:TIGR01931 441 DNFRLPEDPDTPIIMIGPGTGVAPFRAFMQERA-EDGAKGKN----WLFFGNPHFTTDFLYQVEWQNYLKKGVLTKMDLA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 981 YSREpDKPKKYVQDILQEQLAEsVYRALkEQGGHIYVCGDVT-MAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRY 1059
Cdd:TIGR01931 516 FSRD-QAEKIYVQHRIREQGAE-LWQWL-QEGAHIYVCGDAKkMAKDVHQALLDIIAKEGHLDAEEAEEYLTDLRVEKRY 592
|
....*
gi 323635434 1060 HEDIF 1064
Cdd:TIGR01931 593 QRDVY 597
|
|
| cysJ |
PRK10953 |
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit; |
425-1064 |
2.92e-68 |
|
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
Pssm-ID: 182862 [Multi-domain] Cd Length: 600 Bit Score: 240.78 E-value: 2.92e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 425 TILYATETGKSQAYAKTLCEIFKHA-FDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGekfgCALmemrhpnsv 503
Cdd:PRK10953 65 TLISASQTGNARRVAEQLRDDLLAAkLNVNLVNAGDYKFKQIAQEKLLIVVTSTQGEGEPPEEA----VAL--------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 504 qeerksYKVRFNsvssysdsqkssgdgpdlrdnfESAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKM 583
Cdd:PRK10953 132 ------HKFLFS----------------------KKAPKLENTAFAVFGLGDTSYEFFCQAGKDFDSKLAELGAERLLDR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 584 REGD-ELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANNSLISNdrswkrnkfrlTFVAEAPeLTQGLSnVHKKrvs 662
Cdd:PRK10953 184 VDADvEYQAAASEWRARVVDALKSRAPAVAAPSQSVATGAVNEIHTS-----------PYSKEAP-LTASLS-VNQK--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 663 aarLLSRQnlqSPKSSRStIFVRLHTNGsqeLQYQPGDHLGVFPGNHEDLVNALIERL---EDAPpvnqmVKVelleern 739
Cdd:PRK10953 248 ---ITGRN---SEKDVRH-IEIDLGDSG---LRYQPGDALGVWYQNDPALVKELVELLwlkGDEP-----VTV------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 740 talgvisnwtDELRLPpctIFQAFKYYLDITTPpTPLQLQQFASLATSEKekqrLLVL---SKGLQEYeewkwGKNPTIV 816
Cdd:PRK10953 306 ----------DGKTLP---LAEALQWHFELTVN-TANIVENYATLTRSET----LLPLvgdKAALQHY-----AATTPIV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 817 EVLEEFPSiQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYrtrDGEGPIHHGVCSSWL-NRIQADELVPC 895
Cdd:PRK10953 363 DMVRFAPA-QLDAEQLIGLLRPLTPRLYSIASSQAEVENEVHITVGVVRY---DIEGRARAGGASSFLaDRLEEEGEVRV 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 896 FVRGAPSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDiQHKGMNpcpmVLVFGCRQSKIDHIYREETLQAKNKGVFR 975
Cdd:PRK10953 439 FIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAAD-GAPGKN----WLFFGNPHFTEDFLYQVEWQRYVKEGLLT 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 976 ELYTAYSREPDKpKKYVQDILQEQLAEsVYRALkEQGGHIYVCGDVT-MAADVLKAIQRIMTQQGKLSAEDAGVFISRMR 1054
Cdd:PRK10953 514 RIDLAWSRDQKE-KIYVQDKLREQGAE-LWRWI-NDGAHIYVCGDANrMAKDVEQALLEVIAEFGGMDTEAADEFLSELR 590
|
650
....*....|
gi 323635434 1055 DDNRYHEDIF 1064
Cdd:PRK10953 591 VERRYQRDVY 600
|
|
| Flavodoxin_1 |
pfam00258 |
Flavodoxin; |
426-599 |
1.18e-34 |
|
Flavodoxin;
Pssm-ID: 425562 [Multi-domain] Cd Length: 142 Bit Score: 129.41 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 426 ILYATETGKSQAYAKTLCEIFK-HAFDAKVMSMEEYDIV--HLEHETLVLVVTSTFGNGDPPENGEKFgCALMEMRhpns 502
Cdd:pfam00258 1 IFYGSQTGNTEKLAEAIAEGLGeAGFEVDVVDLDDVDETlsEIEEEDLLLVVVSTWGEGEPPDNAKPF-VDWLLLF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 503 vqeerksykvrfnsvssysdsqkssgdgpdlrdNFESAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILK 582
Cdd:pfam00258 76 ---------------------------------GTLEDGDLSGLKYAVFGLGDSGYEGFCGAAKKLDEKLSELGASRVGP 122
|
170 180
....*....|....*....|
gi 323635434 583 MREGDEL---CGQEEAFRTW 599
Cdd:pfam00258 123 LGEGDEDpqeDGLEEAFEAW 142
|
|
| PRK08105 |
PRK08105 |
flavodoxin; Provisional |
418-587 |
2.42e-11 |
|
flavodoxin; Provisional
Pssm-ID: 181230 [Multi-domain] Cd Length: 149 Bit Score: 62.60 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 418 MAKrvkATILYATETGKSQAYAKTLCEIFK-HAFDAKVMSMEEY-DIVHLEHEtLVLVVTSTFGNGDPPENGEKFgcalm 495
Cdd:PRK08105 1 MAK---VGIFVGTVYGNALLVAEEAEAILTaQGHEVTLFEDPELsDWQPYQDE-LVLVVTSTTGQGDLPDSIVPL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 496 emrhpnsvqeerksykvrFNsvssysdsqkssgdgpDLRDNfesAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEEL 575
Cdd:PRK08105 72 ------------------FQ----------------ALKDT---AGYQPNLRYGVIALGDSSYDNFCGAGKQFDALLQEQ 114
|
170
....*....|..
gi 323635434 576 GGERILKMREGD 587
Cdd:PRK08105 115 GAKRVGERLEID 126
|
|
| FldA |
COG0716 |
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ... |
424-490 |
1.12e-04 |
|
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440480 [Multi-domain] Cd Length: 135 Bit Score: 43.35 E-value: 1.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323635434 424 ATILYATETGKSQAYAKTLCEIFKhAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGnGDPPENGEKF 490
Cdd:COG0716 1 ILIVYGSTTGNTEKVAEAIAEALG-AAGVDLFEIEDADLDDLEDYDLLILGTPTWA-GELPDDWEDF 65
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NOS_oxygenase_euk |
cd00795 |
Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by ... |
1-380 |
0e+00 |
|
Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain, which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOS's also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN.
Pssm-ID: 238410 Cd Length: 412 Bit Score: 872.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 1 MGSIMHPSQHARRPEDVRTKGQLFPLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRN 80
Cdd:cd00795 33 LGSIMDPKKLTRRPRDGRPKEELLPQAKDFINQYYSSIKRSGSEAHLARLEEVTKEIEATGTYQLTEDELIFGAKQAWRN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 81 ASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGS 160
Cdd:cd00795 113 APRCIGRIQWSKLQVFDARDCTTAQEMFEAICNHIKYATNKGNLRSAITVFPQRTDGKHDFRIWNSQLIRYAGYKQPDGS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 161 TLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNML 240
Cdd:cd00795 193 IIGDPANVEFTELCIKLGWKPKYGRFDVLPLVLQANGEDPELFEIPPELVLEVPIEHPKYEWFKELGLKWYALPAVSNML 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 241 LEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDH 320
Cdd:cd00795 273 LEIGGLEFTACPFNGWYMGTEIGVRDLCDQQRYNILEEVAKKMGLDTRKTSSLWKDKALVEINVAVLHSFQKANVTIVDH 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 321 HSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPW 380
Cdd:cd00795 353 HSASESFMKHMENEYRARGGCPADWVWIVPPMSGSITPVFHQEMLNYVLSPSYEYQPDPW 412
|
|
| NOS_oxygenase |
cd00575 |
Nitric oxide synthase (NOS) produces nitric oxide (NO) by catalyzing a five-electron ... |
22-377 |
0e+00 |
|
Nitric oxide synthase (NOS) produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. In mammals, there are three distinct NOS isozymes: neuronal (nNOS or NOS-1), cytokine-inducible (iNOS or NOS-2) and endothelial (eNOS or NOS-3) . Nitric oxide synthases are homodimers. In eukaryotes, each monomer has an N-terminal oxygenase domain which binds to the substrate L-Arg, zinc, and to the cofactors heme and 5.6.7.8-(6R)-tetrahydrobiopterin (BH4) . Eukaryotic NOSs also have a C-terminal electron supplying reductase region, which is homologous to cytochrome P450 reductase and binds NADH, FAD and FMN. While prokaryotes can produce NO as a byproduct of denitrification, using a completely different set of enzymes than NOS, a few prokaryotes also have a NOS which consists solely of the NOS oxygenase domain. Prokaryotic NOS binds to the substrate L-Arg, zinc, and to the cofactors heme and tetrahydrofolate.
Pssm-ID: 238321 Cd Length: 356 Bit Score: 783.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 22 QLFPLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDC 101
Cdd:cd00575 1 ELLPQAKDFINQYYSSIKRSGSEAHEARLEEVEKEIEATGTYQLTEEELIYGAKMAWRNAPRCIGRIQWSKLQVFDARDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 102 TTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKP 181
Cdd:cd00575 81 TTAQEMFEAICNHIKYATNGGNIRSAITVFPQRTDGKHDFRIWNSQLIRYAGYKQPDGSIIGDPANVEFTELCIQLGWKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 182 PRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTE 261
Cdd:cd00575 161 KGGRFDVLPLVLQANGEDPELFEIPPELVLEVPIEHPKYEWFAELGLKWYALPAVSNMLLEIGGLEFPAAPFNGWYMGTE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 262 IGVRDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGC 341
Cdd:cd00575 241 IGVRNLCDTQRYNILEKVARKMGLDTRKNSSLWKDRALVELNVAVLHSFQKAGVTIVDHHTAAESFMKHLENEYRARGGC 320
|
330 340 350
....*....|....*....|....*....|....*.
gi 323635434 342 PADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQP 377
Cdd:cd00575 321 PADWVWLVPPMSGSLTPVFHQEMLNYVLSPSFFYQP 356
|
|
| Nitric_oxide_synthase |
cd06202 |
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses ... |
665-1068 |
0e+00 |
|
The ferredoxin-reductase (FNR) like C-terminal domain of the nitric oxide synthase (NOS) fuses with a heme-containing N-terminal oxidase domain. The reductase portion is similar in structure to NADPH dependent cytochrome-450 reductase (CYPOR), having an inserted connecting sub-domain within the FAD binding portion of FNR. NOS differs from CYPOR in a requirement for the cofactor tetrahydrobiopterin and unlike most CYPOR is dimeric. Nitric oxide synthase produces nitric oxide in the conversion of L-arginine to L-citruline. NOS has been implicated in a variety of processes including cytotoxicity, anti-inflamation, neurotransmission, and vascular smooth muscle relaxation.
Pssm-ID: 99799 [Multi-domain] Cd Length: 406 Bit Score: 777.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 665 RLLSRQNLQSPKSSRSTIFVRLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGV 744
Cdd:cd06202 1 KVISRQNLQSPKSSRSTILVKLDTNGAQELHYQPGDHVGIFPANRPELVDALLDRLHDAPPPDQVIKLEVLEERSTALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 745 ISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEYEEWKWGKNPTIVEVLEEFPS 824
Cdd:cd06202 81 IKTWTPHERLPPCTLRQALTRYLDITTPPTPQLLQLLATLATDEKDKERLEVLGKGSSEYEDWKWYKNPNILEVLEEFPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 825 IQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFH 904
Cdd:cd06202 161 LQVPASLLLTQLPLLQPRYYSISSSPDMYPGEIHLTVAVVSYRTRDGQGPVHHGVCSTWLNGLTPGDTVPCFVRSAPSFH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 905 LPRNPQVPCILVGPGTGIAPFRSFWQQRQFDI---QHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAY 981
Cdd:cd06202 241 LPEDPSVPVIMVGPGTGIAPFRSFWQQRQYDLrmsEDPGKKFGDMTLFFGCRNSTIDDIYKEETEEAKNKGVLTEVYTAL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 982 SREPDKPKKYVQDILQEQlAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRYHE 1061
Cdd:cd06202 321 SREPGKPKTYVQDLLKEQ-AESVYDALVREGGHIYVCGDVTMAEDVSQTIQRILAEHGNMSAEEAEEFILKLRDENRYHE 399
|
....*..
gi 323635434 1062 DIFGVTL 1068
Cdd:cd06202 400 DIFGVTL 406
|
|
| NO_synthase |
pfam02898 |
Nitric oxide synthase, oxygenase domain; |
19-380 |
0e+00 |
|
Nitric oxide synthase, oxygenase domain;
Pssm-ID: 460742 Cd Length: 362 Bit Score: 767.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 19 TKGQLFPLAKEFIDQYYSSIKRFgSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDA 98
Cdd:pfam02898 1 PKEELLEEAKEFIEQYYTELKRS-SEEHEARWEEVRAEIEETGTYQHTYEELAYGAKLAWRNSNRCIGRIFWSKLQVFDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 99 RDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQG 178
Cdd:pfam02898 80 RHVTTEEEMFEALCNHIKYATNGGNIRSAITIFPPRTDGKHDFRIWNHQLIRYAGYEQPDGSVIGDPANVEFTELCEKLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 179 WKPPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYM 258
Cdd:pfam02898 160 WKGKGTRFDVLPLVIQANGEDPKLFEIPPELVLEVPIEHPEYEWFAELGLKWYAVPAISNMRLEIGGIEYTAAPFNGWYM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 259 GTEIGVRDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCR 338
Cdd:pfam02898 240 GTEIGARNLADEYRYNLLEKVAKKMGLDTRSNSSLWKDRALVELNVAVLHSFQKAGVTIVDHHTAAEQFMKHEENEQRAG 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 323635434 339 GGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPW 380
Cdd:pfam02898 320 RGCPGDWVWLVPPLSGSTTPVFHQEMDNYILKPNFFYQEDPW 361
|
|
| COG4362 |
COG4362 |
Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism]; |
27-378 |
0e+00 |
|
Nitric oxide synthase, oxygenase domain [Inorganic ion transport and metabolism];
Pssm-ID: 443495 Cd Length: 360 Bit Score: 576.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 27 AKEFIDQYYSSIKRFGSkAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHG 106
Cdd:COG4362 10 AEEFLRQCYKELGKSEE-EVERRLAEVRAEIAATGTYTHTYEELEYGARVAWRNSNRCIGRLFWRSLQVRDRRHVTTPEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 107 MFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRF 186
Cdd:COG4362 89 VFEALVEHLRFATNGGKIRPTITVFAPDQPGRPGVRIWNHQLIRYAGYETEDGSVLGDPASVEFTDACQRLGWRGPRTAF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 187 DVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRD 266
Cdd:COG4362 169 DVLPLVIQVGGEPPRLFEIPRDLVLEVPITHPEYPWFAELGLRWYAVPAISNMRLEIGGIDYPAAPFNGWYMGTEIGARN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 267 YCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWV 346
Cdd:COG4362 249 LADEDRYNLLPKVAERMGLDTSSNRTLWKDRALVELNIAVLHSFKKAGVTIVDHHTASQQFLTFEQREEKAGREVTGDWS 328
|
330 340 350
....*....|....*....|....*....|..
gi 323635434 347 WIVPPMSGSITPVFHQEMLNYRLTPSFEYQPD 378
Cdd:COG4362 329 WLIPPMSGATTHVFHRYYDNEILKPNFFYQDD 360
|
|
| CysJ |
COG0369 |
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ... |
416-1064 |
1.83e-152 |
|
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440138 [Multi-domain] Cd Length: 561 Bit Score: 466.16 E-value: 1.83e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 416 QAMAKRVKATILYATETGKSQAYAKTLCEIFKHA-FDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCAL 494
Cdd:COG0369 21 AAAAAGTPLTILYGSQTGNAEGLAEQLAERAKAAgLAVTLASLDDYKPKDLAKEGLLLIVTSTYGEGEPPDNARAFYEFL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 495 MEMRhpnsvqeerksykvrfnsvssysdsqkssgdgpdlrdnfesAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEE 574
Cdd:COG0369 101 HSKK-----------------------------------------APKLDGLRYAVLGLGDSSYETFCQTGKDFDARLEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 575 LGGERILKMREGDElcGQEEAFRTWAKKVFKAACDVFcvgddvnieKANNSLISNDrswkrnkfrltfVAEAPELTqgls 654
Cdd:COG0369 140 LGATRLLPRVDCDV--DYEEAAEAWLAAVLAALAEAL---------GAAAAAAAAA------------AAAAPAYS---- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 655 nvhKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGSqELQYQPGDHLGVFPGNHEDLVNALIERLEDAPpvNQMVKVEl 734
Cdd:COG0369 193 ---RKNPFPATVLENRELTGRGSAKETRHIEIDLPGS-GLSYEPGDALGVWPENDPALVDELLARLGLDG--DEPVTLD- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 735 leerntalgvisnwtDElrlpPCTIFQAFKYYLDITTPPTPLqLQQFASLATSEKEKQrlLVLSKGLQEYEEWKWGKnpT 814
Cdd:COG0369 266 ---------------GE----PLSLREALTEHLELTRLTPPL-LEKYAELTGNAELAA--LLADEDKAALREYLAGR--Q 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 815 IVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTrdgEGPIHHGVCSSWLNRIQADELVP 894
Cdd:COG0369 322 LLDLLREFPAAELSAEELLELLRPLTPRLYSISSSPKAHPDEVHLTVGVVRYEA---SGRERKGVASTYLADLEEGDTVP 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 895 CFVRGAPSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDiQHKGMNpcpmVLVFGCRQSKIDHIYREETLQAKNKGVF 974
Cdd:COG0369 399 VFVEPNPNFRLPADPDTPIIMIGPGTGIAPFRAFLQEREAR-GASGKN----WLFFGDRHFTTDFLYQTELQAWLKDGVL 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 975 RELYTAYSREpDKPKKYVQDILQEQLAEsVYRALkEQGGHIYVCGDVT-MAADVLKAIQRIMTQQGKLSAEDAGVFISRM 1053
Cdd:COG0369 474 TRLDLAFSRD-QAEKIYVQHRLLEQGAE-LWAWL-EEGAHVYVCGDASrMAKDVDAALLDIIAEHGGLSEEEAEEYLAEL 550
|
650
....*....|.
gi 323635434 1054 RDDNRYHEDIF 1064
Cdd:COG0369 551 RAEKRYQRDVY 561
|
|
| NOS_oxygenase_prok |
cd00794 |
Nitric oxide synthase (NOS) prokaryotic oxygenase domain. NOS produces nitric oxide (NO) by ... |
23-377 |
1.26e-150 |
|
Nitric oxide synthase (NOS) prokaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an intermediate. Nitric oxide synthases are homodimers. Most prokaryotes produce NO as a byproduct of denitrification, using a completely different set of enzymes than NOS. However, a few prokaryotes also have a NOS, consisting solely of the NOS oxygenase domain. Prokaryotic NOS binds to the substrate L-Arg, zinc, and to the cofactors heme and tetrahydrofolate.
Pssm-ID: 238409 Cd Length: 353 Bit Score: 453.43 E-value: 1.26e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 23 LFPLAKEFIDQYYSSIKRFGSKAhmERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCT 102
Cdd:cd00794 2 LFKEARAFLTNMYEELGETGELN--KRLAAVESEIDETGTYTHTTEELVYGAKMAWRNSNRCIGRLFWESLNVRDARDVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 103 TAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTlGDPANVQFTEICIQQGWKPP 182
Cdd:cd00794 80 TEEEVAEALLDHITEATNGGKIRPYITIFAPEAPGKDGPRIWNNQLIRYAGYERPGANI-GDPASAKFTRLAERLGWKGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 183 RGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEI 262
Cdd:cd00794 159 GTNFDVLPLIIQLPGDRPKWFELPNDAVKEVPITHPHYPKIRKLGLKWYAVPIISDMDLEIGGIHYPAAPFNGWYMGTEI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 263 GVRDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCP 342
Cdd:cd00794 239 GARNLADEYRYNLLPKVAEALGLDTLKNRSLWKDRALVELNVAVLHSFKKAGVSIVDHHTAAKQFERFEEREARAGRKVT 318
|
330 340 350
....*....|....*....|....*....|....*
gi 323635434 343 ADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQP 377
Cdd:cd00794 319 GKWSWLIPPLSPATTHIFHRGYDNTEVHPNFFYQK 353
|
|
| CYPOR |
cd06204 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
677-1063 |
2.08e-103 |
|
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99801 [Multi-domain] Cd Length: 416 Bit Score: 331.53 E-value: 2.08e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 677 SSRSTIFVRLHTNGSqELQYQPGDHLGVFPGNHEDLVNALIERLeDAPPVNQMVKVELLEERNTALGVIsnwtdelrLPP 756
Cdd:cd06204 20 SDRSCLHIEFDISGS-GIRYQTGDHLAVWPTNPSEEVERLLKVL-GLDDRDTVISLKSLDEPASKKVPF--------PCP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 757 CTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVL-SKGLQEYEewKWGKNP--TIVEVLEEFPSIQ---MPAT 830
Cdd:cd06204 90 TTYRTALRHYLDITAPVSRQVLAALAQFAPDPEEKERLLKLaSEGKDEYA--KWIVEPhrNLLEVLQDFPSAKptpPPFD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 831 LLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTrdGEGPIHHGVCSSWLNRIQADE------------------- 891
Cdd:cd06204 168 FLIELLPRLQPRYYSISSSSKVHPNRIHITAVVVKYPT--PTGRIIKGVATNWLLALKPALngekpptpyylsgprkkgg 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 892 --LVPCFVRGApSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFdIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAK 969
Cdd:cd06204 246 gsKVPVFVRRS-NFRLPTKPSTPVIMIGPGTGVAPFRGFIQERAA-LKESGKKVGPTLLFFGCRHPDEDFIYKDELEEYA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 970 NKGVFRELYTAYSREPDKpKKYVQDILQEQlAESVYRALKEqGGHIYVCGDV-TMAADVLKAIQRIMTQQGKLSAEDAGV 1048
Cdd:cd06204 324 KLGGLLELVTAFSREQPK-KVYVQHRLAEH-AEQVWELINE-GAYIYVCGDAkNMARDVEKTLLEILAEQGGMTETEAEE 400
|
410
....*....|....*
gi 323635434 1049 FISRMRDDNRYHEDI 1063
Cdd:cd06204 401 YVKKLKTRGRYQEDV 415
|
|
| CYPOR_like |
cd06182 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
665-1064 |
2.83e-103 |
|
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal ferredoxin reducatase (FNR)- like FAD and NAD binding module, an FMN-binding domain, and an additional conecting domain (inserted within the FAD binding region) that orients the FNR and FMN binding domains. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2, which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99779 [Multi-domain] Cd Length: 267 Bit Score: 325.45 E-value: 2.83e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 665 RLLSRQNLQSPKSSRSTIFVRLHTNGSQELQYQPGDHLGVFPGNhedlvnalierledappvnqmvkvelleerntalgv 744
Cdd:cd06182 1 AITVNRKLTPPDSPRSTRHLEFDLSGNSVLKYQPGDHLGVIPPN------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 745 isnwtdelrlppctifqafkyyldittpptPLQlqqfaslatsekekqrllvlskglqeyeewkwgknptivevleefps 824
Cdd:cd06182 45 ------------------------------PLQ----------------------------------------------- 47
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 825 iqmpatllltqlsllqPRYYSISSSPDMYPDEVHLTVAIVSYRtrDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFH 904
Cdd:cd06182 48 ----------------PRYYSIASSPDVDPGEVHLCVRVVSYE--APAGRIRKGVCSNFLAGLQLGAKVTVFIRPAPSFR 109
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 905 LPRNPQVPCILVGPGTGIAPFRSFWQQRQFDiQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSRE 984
Cdd:cd06182 110 LPKDPTTPIIMVGPGTGIAPFRGFLQERAAL-RANGKARGPAWLFFGCRNFASDYLYREELQEALKDGALTRLDVAFSRE 188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 985 PDKPKKYVQDILQEQlAESVYRALKEqGGHIYVCGDVT-MAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRYHEDI 1063
Cdd:cd06182 189 QAEPKVYVQDKLKEH-AEELRRLLNE-GAHIYVCGDAKsMAKDVEDALVKIIAKAGGVDESDAEEYLKELEDEGRYVEDV 266
|
.
gi 323635434 1064 F 1064
Cdd:cd06182 267 W 267
|
|
| FAD_binding_1 |
pfam00667 |
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, ... |
655-883 |
4.56e-96 |
|
FAD binding domain; This domain is found in sulfite reductase, NADPH cytochrome P450 reductase, Nitric oxide synthase and methionine synthase reductase.
Pssm-ID: 395540 [Multi-domain] Cd Length: 219 Bit Score: 304.26 E-value: 4.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 655 NVHKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGSqELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVEL 734
Cdd:pfam00667 1 PFDAKKPFTAPVLSNRELTSPSSDRNCIHVELDISGS-GLTYQTGDHLGVYPPNNEELVEELLERLGLDPKPDTVVLLKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 735 LEErntalgvisnWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLS--KGLQEYEEWKWGKN 812
Cdd:pfam00667 80 LDE----------RVKPPRLPPTTYRQALKYYLDITGPPSKQLLRLLAQFAPEEEEKQRLEFLSsdAGAREYKRWKLNHA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323635434 813 PTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTrDGEGPIHHGVCSSW 883
Cdd:pfam00667 150 PTLLEVLEEFPSVKLPADFLLTQLPQLQPRYYSISSSSKVHPNEVHLTVVVVEYET-DGEGRIHYGVCSNW 219
|
|
| cysJ |
TIGR01931 |
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an ... |
425-1064 |
1.30e-87 |
|
sulfite reductase [NADPH] flavoprotein, alpha-component; This model describes an NADPH-dependent sulfite reductase flavoprotein subunit. Most members of this family are found in Cys biosynthesis gene clusters. The closest homologs below the trusted cutoff are designated as subunits nitrate reductase.
Pssm-ID: 273882 [Multi-domain] Cd Length: 597 Bit Score: 294.68 E-value: 1.30e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 425 TILYATETGKSQAYAKTLCEIFKHA-FDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNsv 503
Cdd:TIGR01931 62 TILYGSQTGNARRLAKRLAEKLEAAgFSVRLSSADDYKFKQLKKERLLLLVISTQGEGEPPEEAISLHKFLHSKKAPK-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 504 qeerksykvrfnsvssysdsqkssgdgpdlrdnfesagpLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKM 583
Cdd:TIGR01931 140 ---------------------------------------LENLRYSVLGLGDSSYEFFCQTGKDFDKRLEELGGKRLLPR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 584 REGDelCGQEEAFRTWAKKVFKAACDVFCVG-DDVNIEKANNSLISNDRSW-KRNKFRltfvaeapeltqglsnvhkkrv 661
Cdd:TIGR01931 181 VDAD--LDYDANAAEWRAGVLTALNEQAKGGaSTPSASETSTPLQTSTSVYsKQNPFR---------------------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 662 saARLLSRQNLQSPKSSRSTIFVRLHTNGSqELQYQPGDHLGVFPGNHEDLVNALIERLEDAPpvNQMVKVElleernta 741
Cdd:TIGR01931 237 --AEVLENQKITGRNSKKDVRHIEIDLEGS-GLHYEPGDALGVWYKNDPALVKEILKLLNLDP--DEKVTIG-------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 742 lgvisnwtDELRlppcTIFQAFKYYLDITTPPTPLqLQQFASLATSEkEKQRLLVLSKGLQEYEEwkwgkNPTIVEVLEE 821
Cdd:TIGR01931 304 --------GKTI----PLFEALITHFELTQNTKPL-LKAYAELTGNK-ELKALIADNEKLKAYIQ-----NTPLIDLIRD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 822 FPSiQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYrtrDGEGPIHHGVCSSWL-NRIQADELVPCFVRGA 900
Cdd:TIGR01931 365 YPA-DLDAEQLISLLRPLTPRLYSISSSQSEVGDEVHLTVGVVRY---QAHGRARLGGASGFLaERLKEGDTVPVYIEPN 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 901 PSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQfDIQHKGMNpcpmVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTA 980
Cdd:TIGR01931 441 DNFRLPEDPDTPIIMIGPGTGVAPFRAFMQERA-EDGAKGKN----WLFFGNPHFTTDFLYQVEWQNYLKKGVLTKMDLA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 981 YSREpDKPKKYVQDILQEQLAEsVYRALkEQGGHIYVCGDVT-MAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRY 1059
Cdd:TIGR01931 516 FSRD-QAEKIYVQHRIREQGAE-LWQWL-QEGAHIYVCGDAKkMAKDVHQALLDIIAKEGHLDAEEAEEYLTDLRVEKRY 592
|
....*
gi 323635434 1060 HEDIF 1064
Cdd:TIGR01931 593 QRDVY 597
|
|
| CyPoR_like |
cd06207 |
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ... |
672-1059 |
4.47e-87 |
|
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99803 [Multi-domain] Cd Length: 382 Bit Score: 286.09 E-value: 4.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 672 LQSPKSSRSTIFVRLHTNGSQeLQYQPGDHLGVFPGNHEDLVNALIERL-EDAppvNQMVKVELLEERNTALGVISnwtd 750
Cdd:cd06207 8 LTPADYDRSTRHIEFDLGGSG-LSYETGDNLGIYPENSDALVDEFLARLgLDG---DDVVRVEPNEQQRGKPPFPE---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 751 elrlpPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLS--KGLQEYEEWKWGknpTIVEVLEEFPSIQMP 828
Cdd:cd06207 80 -----PISVRQLLKKFLDIFGKPTKKFLKLLSQLATDEEEKEDLYKLAsrEGRTEYKRYEKY---TYLEVLKDFPSVRPT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 829 ATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTRDGEgpIHHGVCSSWLNRIQADELVPCFVRgAPSFHLPRN 908
Cdd:cd06207 152 LEQLLELCPLIKPRYYSISSSPLKNPNEVHLLVSLVSWKTPSGR--SRYGLCSSYLAGLKVGQRVTVFIK-KSSFKLPKD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 909 PQVPCILVGPGTGIAPFRSFWQQRQFDIQhKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSREPDKp 988
Cdd:cd06207 229 PKKPIIMVGPGTGLAPFRAFLQERAALLA-QGPEIGPVLLYFGCRHEDKDYLYKEELEEYEKSGVLTTLGTAFSRDQPK- 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323635434 989 KKYVQDILQEQLAEsVYRALKEQGGHIYVCGDVT-MAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRY 1059
Cdd:cd06207 307 KVYVQDLIRENSDL-VYQLLEEGAGVIYVCGSTWkMPPDVQEAFEEILKKHGGGDEELAEKKIEELEERGRY 377
|
|
| SiR |
cd06199 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
665-1064 |
2.98e-85 |
|
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain.
Pssm-ID: 99796 [Multi-domain] Cd Length: 360 Bit Score: 280.27 E-value: 2.98e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 665 RLLSRQNLQSPKSSRSTIFVRLHTNGSQeLQYQPGDHLGVFPGNHEDLVNALIERLEDAPpvNQMVKVELLEERntalgv 744
Cdd:cd06199 1 TVLENRLLTGPGSEKETRHIELDLEGSG-LSYEPGDALGVYPTNDPALVDELLAALGLSG--DEPVSTVGGGTL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 745 isnwtdelrlppcTIFQAFKYYLDITTPPTPLqLQQFASLATsEKEKQRLlvlsKGLQEYEEWKWGKNptIVEVLEEFPs 824
Cdd:cd06199 72 -------------PLREALIKHYEITTLLLAL-LESYAADTG-ALELLAL----AALEAVLAFAELRD--VLDLLPIPP- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 825 IQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTRDGEgpiHHGVCSSWL-NRIQADELVPCFVRGAPSF 903
Cdd:cd06199 130 ARLTAEELLDLLRPLQPRLYSIASSPKAVPDEVHLTVAVVRYESHGRE---RKGVASTFLaDRLKEGDTVPVFVQPNPHF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 904 HLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDiQHKGMNpcpmVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSR 983
Cdd:cd06199 207 RLPEDPDAPIIMVGPGTGIAPFRAFLQEREAT-GAKGKN----WLFFGERHFATDFLYQDELQQWLKDGVLTRLDTAFSR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 984 epDKPKK-YVQDILQEQLAEsVYRALkEQGGHIYVCGDVT-MAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRYHE 1061
Cdd:cd06199 282 --DQAEKvYVQDRMREQGAE-LWAWL-EEGAHFYVCGDAKrMAKDVDAALLDIIATEGGMDEEEAEAYLKELKKEKRYQR 357
|
...
gi 323635434 1062 DIF 1064
Cdd:cd06199 358 DVY 360
|
|
| bifunctional_CYPOR |
cd06206 |
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ... |
660-1064 |
3.54e-77 |
|
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase (CYPOR). NADPH cytochrome p450 reductase serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99802 [Multi-domain] Cd Length: 384 Bit Score: 259.11 E-value: 3.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 660 RVSAARLLSrqnlqSPKSSRST--IFVRLHTNGSqelqYQPGDHLGVFPGNHEDLVNALIERLEDAPpvNQMVKVELLEE 737
Cdd:cd06206 1 TVVENRELT-----APGVGPSKrhLELRLPDGMT----YRAGDYLAVLPRNPPELVRRALRRFGLAW--DTVLTISASGS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 738 RntalgvisnwtdeLRLP---PCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKglQEYEEWKWGKNPT 814
Cdd:cd06206 70 A-------------TGLPlgtPISVSELLSSYVELSQPATRRQLAALAEATRCPDTKALLERLAG--EAYAAEVLAKRVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 815 IVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTRDGEGPiHHGVCSSWLNRIQADELVP 894
Cdd:cd06206 135 VLDLLERFPSIALPLATFLAMLPPMRPRQYSISSSPLVDPGHATLTVSVLDAPALSGQGR-YRGVASSYLSSLRPGDSIH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 895 CFVRGA-PSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDIQHkGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGV 973
Cdd:cd06206 214 VSVRPShSAFRPPSDPSTPLIMIAAGTGLAPFRGFLQERAALLAQ-GRKLAPALLFFGCRHPDHDDLYRDELEEWEAAGV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 974 FrELYTAYSREPDKPKKYVQDILQEQLAESVyrALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKL----SAEDAGVF 1049
Cdd:cd06206 293 V-SVRRAYSRPPGGGCRYVQDRLWAEREEVW--ELWEQGARVYVCGDGRMAPGVREVLKRIYAEKDERgggsDDEEAEEW 369
|
410
....*....|....*
gi 323635434 1050 ISRMRDDNRYHEDIF 1064
Cdd:cd06206 370 LEELRNKGRYATDVF 384
|
|
| cysJ |
PRK10953 |
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit; |
425-1064 |
2.92e-68 |
|
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
Pssm-ID: 182862 [Multi-domain] Cd Length: 600 Bit Score: 240.78 E-value: 2.92e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 425 TILYATETGKSQAYAKTLCEIFKHA-FDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGekfgCALmemrhpnsv 503
Cdd:PRK10953 65 TLISASQTGNARRVAEQLRDDLLAAkLNVNLVNAGDYKFKQIAQEKLLIVVTSTQGEGEPPEEA----VAL--------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 504 qeerksYKVRFNsvssysdsqkssgdgpdlrdnfESAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKM 583
Cdd:PRK10953 132 ------HKFLFS----------------------KKAPKLENTAFAVFGLGDTSYEFFCQAGKDFDSKLAELGAERLLDR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 584 REGD-ELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANNSLISNdrswkrnkfrlTFVAEAPeLTQGLSnVHKKrvs 662
Cdd:PRK10953 184 VDADvEYQAAASEWRARVVDALKSRAPAVAAPSQSVATGAVNEIHTS-----------PYSKEAP-LTASLS-VNQK--- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 663 aarLLSRQnlqSPKSSRStIFVRLHTNGsqeLQYQPGDHLGVFPGNHEDLVNALIERL---EDAPpvnqmVKVelleern 739
Cdd:PRK10953 248 ---ITGRN---SEKDVRH-IEIDLGDSG---LRYQPGDALGVWYQNDPALVKELVELLwlkGDEP-----VTV------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 740 talgvisnwtDELRLPpctIFQAFKYYLDITTPpTPLQLQQFASLATSEKekqrLLVL---SKGLQEYeewkwGKNPTIV 816
Cdd:PRK10953 306 ----------DGKTLP---LAEALQWHFELTVN-TANIVENYATLTRSET----LLPLvgdKAALQHY-----AATTPIV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 817 EVLEEFPSiQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYrtrDGEGPIHHGVCSSWL-NRIQADELVPC 895
Cdd:PRK10953 363 DMVRFAPA-QLDAEQLIGLLRPLTPRLYSIASSQAEVENEVHITVGVVRY---DIEGRARAGGASSFLaDRLEEEGEVRV 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 896 FVRGAPSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDiQHKGMNpcpmVLVFGCRQSKIDHIYREETLQAKNKGVFR 975
Cdd:PRK10953 439 FIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAAD-GAPGKN----WLFFGNPHFTEDFLYQVEWQRYVKEGLLT 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 976 ELYTAYSREPDKpKKYVQDILQEQLAEsVYRALkEQGGHIYVCGDVT-MAADVLKAIQRIMTQQGKLSAEDAGVFISRMR 1054
Cdd:PRK10953 514 RIDLAWSRDQKE-KIYVQDKLREQGAE-LWRWI-NDGAHIYVCGDANrMAKDVEQALLEVIAEFGGMDTEAADEFLSELR 590
|
650
....*....|
gi 323635434 1055 DDNRYHEDIF 1064
Cdd:PRK10953 591 VERRYQRDVY 600
|
|
| methionine_synthase_red |
cd06203 |
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for ... |
690-1063 |
7.20e-67 |
|
Human methionine synthase reductase (MSR) restores methionine sythase which is responsible for the regeneration of methionine from homocysteine, as well as the coversion of methyltetrahydrofolate to tetrahydrofolate. In MSR, electrons are transferred from NADPH to FAD to FMN to cob(II)alamin. MSR resembles proteins of the cytochrome p450 family including nitric oxide synthase, the alpha subunit of sulfite reductase, but contains an extended hinge region. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPORs resemble ferredoxin reductase (FNR) but have a connecting subdomain inserted within the flavin binding region, which helps orient the FMN binding doamin with the FNR module. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99800 [Multi-domain] Cd Length: 398 Bit Score: 230.67 E-value: 7.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 690 GSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLE--ERNTAlgvisnwtdelRLPP-----CTIFQA 762
Cdd:cd06203 25 SPTGFDYQPGDTIGILPPNTASEVESLLKRLGLLEQADQPCEVKVVPntKKKNA-----------KVPVhipkvVTLRTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 763 FKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLS--KGLQEYEEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQ 840
Cdd:cd06203 94 LTWCLDIRAIPKKPLLRALAEFTSDDNEKRRLEELCskQGSEDYTDFVRKRGLSLLDLLEAFPSCRPPLSLLIEHLPRLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 841 PRYYSISSSPDMYPDEVHLTVAIVSYRTRdgegpihhGVCSSWLN--RIQADEL---VPCFVRGAPSFHLP-RNPQVPCI 914
Cdd:cd06203 174 PRPYSIASSPLEGPGKLRFIFSVVEFPAK--------GLCTSWLEslCLSASSHgvkVPFYLRSSSRFRLPpDDLRRPII 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 915 LVGPGTGIAPFRSFWQQRQFDIQHKGMNPC-PMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSREPD--KPKKY 991
Cdd:cd06203 246 MVGPGTGVAPFLGFLQHREKLKESHTETVFgEAWLFFGCRHRDRDYLFRDELEEFLEEGILTRLIVAFSRDENdgSTPKY 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 323635434 992 VQDILQEQlAESVYRALKEQGGHIYVCGDV-TMAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRYHEDI 1063
Cdd:cd06203 326 VQDKLEER-GKKLVDLLLNSNAKIYVCGDAkGMAKDVRDTFVDILSKELGLDKLEAKKLLARLRKEDRYLEDV 397
|
|
| PRK06214 |
PRK06214 |
sulfite reductase subunit alpha; |
664-1064 |
3.14e-65 |
|
sulfite reductase subunit alpha;
Pssm-ID: 235745 [Multi-domain] Cd Length: 530 Bit Score: 230.34 E-value: 3.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 664 ARLLSRQNLQSPKSSRSTIFVRLHTNGSQeLQYQPGDHLGVFPGNHEDLVNALIERLEDAP--PVNQMVKVELLEErNTA 741
Cdd:PRK06214 171 ATFLSRRRLNKPGSEKETWHVEIDLAGSG-LDYEVGDSLGLFPANDPALVDAVIAALGAPPefPIGGKTLREALLE-DVS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 742 LGvisnwtdelrlppctifqafkyyldittpPTPLQLQQFASLATSEKEKQRLLVLSKGlqeyeEWKWGKNPT--IVEVL 819
Cdd:PRK06214 249 LG-----------------------------PAPDGLFELLSYITGGAARKKARALAAG-----EDPDGDAATldVLAAL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 820 EEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTRDGEgpiHHGVCSSWL-NRIQADELVPCFVR 898
Cdd:PRK06214 295 EKFPGIRPDPEAFVEALDPLQPRLYSISSSPKATPGRVSLTVDAVRYEIGSRL---RLGVASTFLgERLAPGTRVRVYVQ 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 899 GAPSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQfDIQHKGMNpcpmVLVFGCRQSKIDHIYREETLQAKNKGVFRELY 978
Cdd:PRK06214 372 KAHGFALPADPNTPIIMVGPGTGIAPFRAFLHERA-ATKAPGRN----WLFFGHQRSATDFFYEDELNGLKAAGVLTRLS 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 979 TAYSREPDKpKKYVQDILQEQLAEsVYRALkEQGGHIYVCGDVT-MAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDN 1057
Cdd:PRK06214 447 LAWSRDGEE-KTYVQDRMRENGAE-LWKWL-EEGAHFYVCGDAKrMAKDVERALVDIVAQFGGRSPDEAVAFVAELKKAG 523
|
....*..
gi 323635434 1058 RYHEDIF 1064
Cdd:PRK06214 524 RYQADVY 530
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
841-1044 |
7.60e-36 |
|
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99778 [Multi-domain] Cd Length: 223 Bit Score: 135.65 E-value: 7.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 841 PRYYSISSSPDMyPDEVHLTVAIVSyrtrdgegpihHGVCSSWLNRIQADELVPCFVRGAPSFhLPRNPQVPCILVGPGT 920
Cdd:cd00322 41 RRAYSIASSPDE-EGELELTVKIVP-----------GGPFSAWLHDLKPGDEVEVSGPGGDFF-LPLEESGPVVLIAGGI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 921 GIAPFRSFWQQRQFDIqhkgmNPCPMVLVFGCRQSKiDHIYREETLQAKNKGVFRELYTAYSREPDKPKKYVQDILQEQL 1000
Cdd:cd00322 108 GITPFRSMLRHLAADK-----PGGEITLLYGARTPA-DLLFLDELEELAKEGPNFRLVLALSRESEAKLGPGGRIDREAE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 323635434 1001 AESvyRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAE 1044
Cdd:cd00322 182 ILA--LLPDDSGALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
|
|
| Flavodoxin_1 |
pfam00258 |
Flavodoxin; |
426-599 |
1.18e-34 |
|
Flavodoxin;
Pssm-ID: 425562 [Multi-domain] Cd Length: 142 Bit Score: 129.41 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 426 ILYATETGKSQAYAKTLCEIFK-HAFDAKVMSMEEYDIV--HLEHETLVLVVTSTFGNGDPPENGEKFgCALMEMRhpns 502
Cdd:pfam00258 1 IFYGSQTGNTEKLAEAIAEGLGeAGFEVDVVDLDDVDETlsEIEEEDLLLVVVSTWGEGEPPDNAKPF-VDWLLLF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 503 vqeerksykvrfnsvssysdsqkssgdgpdlrdNFESAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILK 582
Cdd:pfam00258 76 ---------------------------------GTLEDGDLSGLKYAVFGLGDSGYEGFCGAAKKLDEKLSELGASRVGP 122
|
170 180
....*....|....*....|
gi 323635434 583 MREGDEL---CGQEEAFRTW 599
Cdd:pfam00258 123 LGEGDEDpqeDGLEEAFEAW 142
|
|
| SiR_like2 |
cd06201 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
841-1064 |
1.02e-32 |
|
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99798 [Multi-domain] Cd Length: 289 Bit Score: 128.99 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 841 PRYYSISSSpdmypdevhltvaivsyrTRDGEGPI----H-HGVCSSWLNRIQADELVPCFVRGAPSFHLPRNpQVPCIL 915
Cdd:cd06201 100 PRFYSLASS------------------SSDGFLEIcvrkHpGGLCSGYLHGLKPGDTIKAFIRPNPSFRPAKG-AAPVIL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 916 VGPGTGIAPFRSFwqQRQFDIQHkgmnpcPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSREPDkpKKYVQDI 995
Cdd:cd06201 161 IGAGTGIAPLAGF--IRANAARR------PMHLYWGGRDPASDFLYEDELDQYLADGRLTQLHTAFSRTPD--GAYVQDR 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 323635434 996 LQEQlAESVyRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGklsaedAGVFISRMrdDNRYHEDIF 1064
Cdd:cd06201 231 LRAD-AERL-RRLIEDGAQIMVCGSRAMAQGVAAVLEEILAPQP------LSLDELKL--QGRYAEDVY 289
|
|
| SiR_like1 |
cd06200 |
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ... |
841-1064 |
1.48e-29 |
|
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99797 Cd Length: 245 Bit Score: 118.15 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 841 PRYYSISSSPDmypD-EVHLTVAivsyRTRDGEGpiHHGVCSSWLNRIQAD-ELVPCFVRGAPSFHLPrNPQVPCILVGP 918
Cdd:cd06200 48 HREYSIASLPA---DgALELLVR----QVRHADG--GLGLGSGWLTRHAPIgASVALRLRENPGFHLP-DDGRPLILIGN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 919 GTGIAPFRSFWQQRQFDIQHKGMnpcpmvLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSREpDKPKKYVQDILQE 998
Cdd:cd06200 118 GTGLAGLRSHLRARARAGRHRNW------LLFGERQAAHDFFCREELEAWQAAGHLARLDLAFSRD-QAQKRYVQDRLRA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323635434 999 QLAEsvYRALKEQGGHIYVCGDV-TMAADVLKAIQRIMTQQGKlsaedagvfiSRMRDDNRYHEDIF 1064
Cdd:cd06200 191 AADE--LRAWVAEGAAIYVCGSLqGMAPGVDAVLDEILGEEAV----------EALLAAGRYRRDVY 245
|
|
| CYPOR_like_FNR |
cd06208 |
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but ... |
841-1060 |
1.63e-26 |
|
These ferredoxin reductases are related to the NADPH cytochrome p450 reductases (CYPOR), but lack the FAD-binding region connecting sub-domain. Ferredoxin-NADP+ reductase (FNR) is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins, such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2, which then transfers two electrons and a proton to NADP+ to form NADPH. CYPOR serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases, sulfite reducatase, and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal FNR-like FAD and NAD binding module, an FMN-binding domain, and an additional connecting domain (inserted within the FAD binding region) that orients the FNR and FMN -binding domains. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99804 [Multi-domain] Cd Length: 286 Bit Score: 110.49 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 841 PRYYSISSSPDM---YPDEVHLTVAIVSYrTRDGEGPIHHGVCSSWLNRIQADELVpcFVRGaPS---FHLPRNPQVPCI 914
Cdd:cd06208 64 LRLYSIASSRYGddgDGKTLSLCVKRLVY-TDPETDETKKGVCSNYLCDLKPGDDV--QITG-PVgktMLLPEDPNATLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 915 LVGPGTGIAPFRSFWQQRQF----DIQHKGMnpcpMVLVFGCRQSKiDHIYREE--TLQAKNKGVFReLYTAYSREP--- 985
Cdd:cd06208 140 MIATGTGIAPFRSFLRRLFRekhaDYKFTGL----AWLFFGVPNSD-SLLYDDEleKYPKQYPDNFR-IDYAFSREQkna 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323635434 986 DKPKKYVQDILQEQlAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMtqqGKLSAEDAgvFISRMRDDNRYH 1060
Cdd:cd06208 214 DGGKMYVQDRIAEY-AEEIWNLLDKDNTHVYICGLKGMEPGVDDALTSVA---EGGLAWEE--FWESLKKKGRWH 282
|
|
| NAD_binding_1 |
pfam00175 |
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
915-1029 |
2.82e-26 |
|
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.
Pssm-ID: 425503 [Multi-domain] Cd Length: 109 Bit Score: 104.26 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 915 LVGPGTGIAPFRSFWQQRQFDIQHKGmnpcPMVLVFGCRQSKiDHIYREE--TLQAKNKGVFReLYTAYSREPDKP---K 989
Cdd:pfam00175 1 MIAGGTGIAPVRSMLRAILEDPKDPT----QVVLVFGNRNED-DILYREEldELAEKHPGRLT-VVYVVSRPEAGWtggK 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 323635434 990 KYVQDILQEQLAEsvyraLKEQGGHIYVCGDVTMAADVLK 1029
Cdd:pfam00175 75 GRVQDALLEDHLS-----LPDEETHVYVCGPPGMIKAVRK 109
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
842-1060 |
4.67e-16 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 78.68 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 842 RYYSISSSPDmypdEVHLTVAIVsyRTRDGEGpihhgvcSSWLN-RIQA-DELvpcFVRGaPS--FHLPRNPQVPCILVG 917
Cdd:COG1018 53 RAYSLSSAPG----DGRLEITVK--RVPGGGG-------SNWLHdHLKVgDTL---EVSG-PRgdFVLDPEPARPLLLIA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 918 PGTGIAPFRSFWQqrqfDIQHKGMNPcPMVLVFGCRQSKiDHIYREE--TLQAKNKGVfrELYTAYSREPDKPKKYV-QD 994
Cdd:COG1018 116 GGIGITPFLSMLR----TLLARGPFR-PVTLVYGARSPA-DLAFRDEleALAARHPRL--RLHPVLSREPAGLQGRLdAE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323635434 995 ILQEQLAEsvyralkEQGGHIYVCGDVTMAADVLKAiqrimtqqgklsAEDAGVfisrmrDDNRYH 1060
Cdd:COG1018 188 LLAALLPD-------PADAHVYLCGPPPMMEAVRAA------------LAELGV------PEERIH 228
|
|
| PLN03116 |
PLN03116 |
ferredoxin--NADP+ reductase; Provisional |
841-1064 |
7.02e-14 |
|
ferredoxin--NADP+ reductase; Provisional
Pssm-ID: 215586 [Multi-domain] Cd Length: 307 Bit Score: 73.59 E-value: 7.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 841 PRYYSISSSpdMYPDEVHLTVA------IVSYRTRDG-EGPIHHGVCSSWL-NRIQADELVpcfVRGaPS---FHLP-RN 908
Cdd:PLN03116 81 VRLYSIAST--RYGDDFDGKTAslcvrrAVYYDPETGkEDPAKKGVCSNFLcDAKPGDKVQ---ITG-PSgkvMLLPeED 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 909 PQVPCILVGPGTGIAPFRSFWqQRQF-----DIQHKGMnpcpMVLVFGCRQSKiDHIYREE--TLQAKNKGVFReLYTAY 981
Cdd:PLN03116 155 PNATHIMVATGTGIAPFRGFL-RRMFmedvpAFKFGGL----AWLFLGVANSD-SLLYDDEfeRYLKDYPDNFR-YDYAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 982 SREpDKPKK----YVQDILqEQLAESVYRALkEQGGHIYVCGDVTMAADVLKAIQRIMTQQGklsaEDAGVFISRMRDDN 1057
Cdd:PLN03116 228 SRE-QKNKKggkmYVQDKI-EEYSDEIFKLL-DNGAHIYFCGLKGMMPGIQDTLKRVAEERG----ESWEEKLSGLKKNK 300
|
....*..
gi 323635434 1058 RYHEDIF 1064
Cdd:PLN03116 301 QWHVEVY 307
|
|
| FNR1 |
cd06195 |
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ... |
842-1033 |
2.27e-13 |
|
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99792 [Multi-domain] Cd Length: 241 Bit Score: 71.06 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 842 RYYSISSSPDmypdEVHLTVAIVsyRTRDGEgpihhgvCSSWLNRIQA-DELvpcFVRGAPSFHLPRNPQVPC---ILVG 917
Cdd:cd06195 45 RAYSIASAPY----EENLEFYII--LVPDGP-------LTPRLFKLKPgDTI---YVGKKPTGFLTLDEVPPGkrlWLLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 918 PGTGIAPFRSFWQQ----RQFDiqhkgmnpcPMVLVFGCRQSKiDHIYREE--TLQAKNKGVFReLYTAYSREPDKP--K 989
Cdd:cd06195 109 TGTGIAPFLSMLRDleiwERFD---------KIVLVHGVRYAE-ELAYQDEieALAKQYNGKFR-YVPIVSREKENGalT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 323635434 990 KYVQDILQ-EQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQR 1033
Cdd:cd06195 178 GRIPDLIEsGELEEHAGLPLDPETSHVMLCGNPQMIDDTQELLKE 222
|
|
| PLN03115 |
PLN03115 |
ferredoxin--NADP(+) reductase; Provisional |
842-1045 |
5.83e-12 |
|
ferredoxin--NADP(+) reductase; Provisional
Pssm-ID: 215585 [Multi-domain] Cd Length: 367 Bit Score: 68.87 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 842 RYYSISSS-PDMYPDE--VHLTVAIVSYRTRDGEgpIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGP 918
Cdd:PLN03115 146 RLYSIASSaLGDFGDSktVSLCVKRLVYTNDQGE--IVKGVCSNFLCDLKPGAEVKITGPVGKEMLMPKDPNATIIMLAT 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 919 GTGIAPFRSF-WQ---QRQFDIQHKGMnpcpMVLVFGCRQSKiDHIYREE--TLQAKNKGVFRELYtAYSREPDKP---K 989
Cdd:PLN03115 224 GTGIAPFRSFlWKmffEKHDDYKFNGL----AWLFLGVPTSS-SLLYKEEfeKMKEKAPENFRLDF-AVSREQTNAkgeK 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 323635434 990 KYVQDILQEqLAESVYRALKEQGGHIYVCGDVTMAadvlKAIQRIMTQqgkLSAED 1045
Cdd:PLN03115 298 MYIQTRMAE-YAEELWELLKKDNTYVYMCGLKGME----KGIDDIMVS---LAAKD 345
|
|
| PRK08105 |
PRK08105 |
flavodoxin; Provisional |
418-587 |
2.42e-11 |
|
flavodoxin; Provisional
Pssm-ID: 181230 [Multi-domain] Cd Length: 149 Bit Score: 62.60 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 418 MAKrvkATILYATETGKSQAYAKTLCEIFK-HAFDAKVMSMEEY-DIVHLEHEtLVLVVTSTFGNGDPPENGEKFgcalm 495
Cdd:PRK08105 1 MAK---VGIFVGTVYGNALLVAEEAEAILTaQGHEVTLFEDPELsDWQPYQDE-LVLVVTSTTGQGDLPDSIVPL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 496 emrhpnsvqeerksykvrFNsvssysdsqkssgdgpDLRDNfesAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEEL 575
Cdd:PRK08105 72 ------------------FQ----------------ALKDT---AGYQPNLRYGVIALGDSSYDNFCGAGKQFDALLQEQ 114
|
170
....*....|..
gi 323635434 576 GGERILKMREGD 587
Cdd:PRK08105 115 GAKRVGERLEID 126
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
841-1039 |
2.71e-11 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 64.88 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 841 PRYYSISSSPDMyPDEVHLTVAIVsyrtrdgegpihhGVCSSWLNRIQADELVpcFVRGaP---SFHLPRNPQvPCILVG 917
Cdd:COG0543 42 RRPFSIASAPRE-DGTIELHIRVV-------------GKGTRALAELKPGDEL--DVRG-PlgnGFPLEDSGR-PVLLVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 918 PGTGIAPFRSFwqqrqfdIQHKGMNPCPMVLVFGCRqSKIDHIYREEtlqaknkgvFREL----YTAYSREPDKPKK-YV 992
Cdd:COG0543 104 GGTGLAPLRSL-------AEALLARGRRVTLYLGAR-TPEDLYLLDE---------LEALadfrVVVTTDDGWYGRKgFV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 323635434 993 QDILQEQLAESVYRalkeqggHIYVCGDVTMaadvLKAIQRIMTQQG 1039
Cdd:COG0543 167 TDALKELLAEDSGD-------DVYACGPPPM----MKAVAELLLERG 202
|
|
| O2ase_reductase_like |
cd06187 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
841-1030 |
4.88e-08 |
|
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.
Pssm-ID: 99784 [Multi-domain] Cd Length: 224 Bit Score: 54.91 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 841 PRYYSISSSPDmyPD-EVHLTVAIVSyrtrdgegpihHGVCSSWL-NRIQADELVpcfVRGAP--SFHLPRNPQVPCILV 916
Cdd:cd06187 41 WRAYSPANPPN--EDgEIEFHVRAVP-----------GGRVSNALhDELKVGDRV---RLSGPygTFYLRRDHDRPVLCI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 917 GPGTGIAPFRSFWQqrqfDIQHKGMNPcPMVLVFGCRQSkiDHIYREETLQ--AKNKGVFReLYTAYSREPDKPkkyvqD 994
Cdd:cd06187 105 AGGTGLAPLRAIVE----DALRRGEPR-PVHLFFGARTE--RDLYDLEGLLalAARHPWLR-VVPVVSHEEGAW-----T 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 323635434 995 ILQEQLAESVYRALKEQGGH-IYVCGDVTMAADVLKA 1030
Cdd:cd06187 172 GRRGLVTDVVGRDGPDWADHdIYICGPPAMVDATVDA 208
|
|
| FNR_iron_sulfur_binding_3 |
cd06217 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
842-1029 |
5.87e-08 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99813 [Multi-domain] Cd Length: 235 Bit Score: 54.96 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 842 RYYSISSSPDMyPDEVHLTVAivsyRTRDGEgpihhgvCSSWLNRIQA--DELvpcFVRGaP--SFHLPRNPQVPCILVG 917
Cdd:cd06217 51 RSYSIASSPTQ-RGRVELTVK----RVPGGE-------VSPYLHDEVKvgDLL---EVRG-PigTFTWNPLHGDPVVLLA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 918 PGTGIAPFRSFWQQRqfdiQHKGMNPcPMVLVFGCRQSKiDHIYREETLQ-AKNKGVFrELYTAYSREPDK----PKKYV 992
Cdd:cd06217 115 GGSGIVPLMSMIRYR----RDLGWPV-PFRLLYSARTAE-DVIFRDELEQlARRHPNL-HVTEALTRAAPAdwlgPAGRI 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 323635434 993 QDILQEQLAESVyralkeQGGHIYVCGDVTMAADVLK 1029
Cdd:cd06217 188 TADLIAELVPPL------AGRRVYVCGPPAFVEAATR 218
|
|
| FNR_iron_sulfur_binding_2 |
cd06216 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
842-1027 |
7.39e-07 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99812 [Multi-domain] Cd Length: 243 Bit Score: 51.46 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 842 RYYSISSSPDMYPDEVHLTVAIVSyrtrdgegpihHGVCSSWL-NRIQADELVPCfvrGAPS--FHLPRNPQVPCILVGP 918
Cdd:cd06216 65 RSYSLSSSPTQEDGTITLTVKAQP-----------DGLVSNWLvNHLAPGDVVEL---SQPQgdFVLPDPLPPRLLLIAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 919 GTGIAPFRSFWQqrqfdiQHKGMNPCPMVLVFGCRQSKIDHIYREE--TLQAKNKGV-FRELYTAYSREpdkpkkyvQDI 995
Cdd:cd06216 131 GSGITPVMSMLR------TLLARGPTADVVLLYYARTREDVIFADElrALAAQHPNLrLHLLYTREELD--------GRL 196
|
170 180 190
....*....|....*....|....*....|..
gi 323635434 996 LQEQLAESVyraLKEQGGHIYVCGDVTMAADV 1027
Cdd:cd06216 197 SAAHLDAVV---PDLADRQVYACGPPGFLDAA 225
|
|
| BenDO_FAD_NAD |
cd06209 |
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ... |
842-1023 |
1.02e-06 |
|
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group.
Pssm-ID: 99805 [Multi-domain] Cd Length: 228 Bit Score: 51.06 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 842 RYYSISSSPDmypdEVHLTVAIvsyrtRDGEGpihhGVCSSWL-NRIQADELVPCfvrGAP--SFHLpRNPQVPCILVGP 918
Cdd:cd06209 48 RSYSFSSAPG----DPRLEFLI-----RLLPG----GAMSSYLrDRAQPGDRLTL---TGPlgSFYL-REVKRPLLMLAG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 919 GTGIAPFRSFWQQrqfdIQHKGMNPcPMVLVFGCRQS----KIDHIyreETLQAKNKGvFRELYTAYSREPDKPKK-YVQ 993
Cdd:cd06209 111 GTGLAPFLSMLDV----LAEDGSAH-PVHLVYGVTRDadlvELDRL---EALAERLPG-FSFRTVVADPDSWHPRKgYVT 181
|
170 180 190
....*....|....*....|....*....|
gi 323635434 994 DILQEqlaesvyRALKEQGGHIYVCGDVTM 1023
Cdd:cd06209 182 DHLEA-------EDLNDGDVDVYLCGPPPM 204
|
|
| PRK09004 |
PRK09004 |
FMN-binding protein MioC; Provisional |
465-580 |
1.23e-06 |
|
FMN-binding protein MioC; Provisional
Pssm-ID: 181608 [Multi-domain] Cd Length: 146 Bit Score: 49.06 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 465 LEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRhpnsvqeerksykvrfnsvssysdsqkssgdgPDLrdnfesagplA 544
Cdd:PRK09004 44 LSASGLWLIVTSTHGAGDLPDNLQPFFEELQEQK--------------------------------PDL----------S 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 323635434 545 NVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERI 580
Cdd:PRK09004 82 QVRFAAIGIGSSEYDTFCGAIDKLEQLLKAKGAKQI 117
|
|
| PRK06703 |
PRK06703 |
flavodoxin; Provisional |
423-601 |
1.70e-06 |
|
flavodoxin; Provisional
Pssm-ID: 235854 [Multi-domain] Cd Length: 151 Bit Score: 48.99 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 423 KATILYATETGKSQAYAKTLCEIFK-HAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFgcalmemrhpn 501
Cdd:PRK06703 3 KILIAYASMSGNTEDIADLIKVSLDaFDHEVVLQEMDGMDAEELLAYDGIILGSYTWGDGDLPYEAEDF----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 502 svQEERKSYKvrfnsvssysdsqkssgdgpdlrdnfesagpLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGE--- 578
Cdd:PRK06703 72 --HEDLENID-------------------------------LSGKKVAVFGSGDTAYPLFCEAVTIFEERLVERGAElvq 118
|
170 180 190
....*....|....*....|....*....|
gi 323635434 579 RILKMR-----EGDELCGQE--EAFRTWAK 601
Cdd:PRK06703 119 EGLKIElapetDEDVEKCSNfaIAFAEKFA 148
|
|
| NADH_quinone_reductase |
cd06188 |
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ... |
842-1031 |
4.56e-06 |
|
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain of this group typically contains an iron-sulfur cluster binding domain.
Pssm-ID: 99785 [Multi-domain] Cd Length: 283 Bit Score: 49.61 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 842 RYYSISSSPDMyPDEVHLTVAIVSyrTRDGEGPIHHGVCSSWLNRIQADELVPcfVRGAPSFHLPRNPQVPCILVGPGTG 921
Cdd:cd06188 87 RAYSLANYPAE-EGELKLNVRIAT--PPPGNSDIPPGIGSSYIFNLKPGDKVT--ASGPFGEFFIKDTDREMVFIGGGAG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 922 IAPFRSFWQQrqfdiQHKGMNPC-PMVLVFGCRqSKIDHIYREE--TLQAKNKGvFReLYTAYSR---EPDK--PKKYVQ 993
Cdd:cd06188 162 MAPLRSHIFH-----LLKTLKSKrKISFWYGAR-SLKELFYQEEfeALEKEFPN-FK-YHPVLSEpqpEDNWdgYTGFIH 233
|
170 180 190
....*....|....*....|....*....|....*...
gi 323635434 994 DILQEQLAEsvyRALKEQGGHIYVCGDVTMAADVLKAI 1031
Cdd:cd06188 234 QVLLENYLK---KHPAPEDIEFYLCGPPPMNSAVIKML 268
|
|
| FNR_iron_sulfur_binding |
cd06191 |
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
842-1064 |
2.12e-05 |
|
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR was intially identified as a chloroplast reductase activity catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methnae assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99788 [Multi-domain] Cd Length: 231 Bit Score: 47.14 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 842 RYYSISSSPdmYPDEVHLTVAIVsyrtrdgEGpihhGVCSSWLNRIqADELVPCFVRGAPS-FHLPRNPQVPCILVGPGT 920
Cdd:cd06191 47 RCYSLCSSP--APDEISITVKRV-------PG----GRVSNYLREH-IQPGMTVEVMGPQGhFVYQPQPPGRYLLVAAGS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 921 GIAPFRSFWQQRqfdiqHKGMNPCPMVLVFGCRQSKiDHIYREETLQAKNKGVFRELYTAYSRE-PDKPKKYVQDILQEQ 999
Cdd:cd06191 113 GITPLMAMIRAT-----LQTAPESDFTLIHSARTPA-DMIFAQELRELADKPQRLRLLCIFTREtLDSDLLHGRIDGEQS 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323635434 1000 LAESVYRALKEQggHIYVCGdvtmAADVLKAIQRIMTQQGklsaedagvfisrmRDDNRYHEDIF 1064
Cdd:cd06191 187 LGAALIPDRLER--EAFICG----PAGMMDAVETALKELG--------------MPPERIHTERF 231
|
|
| FNR_N-term_Iron_sulfur_binding |
cd06194 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
841-1023 |
4.57e-05 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99791 [Multi-domain] Cd Length: 222 Bit Score: 46.11 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 841 PRYYSISSSPDMyPDEVHLTVAIVsyrtrdgegpiHHGVCSSWL-NRIQADELVPcfVRG--APSFHLPRNPQVPCILVG 917
Cdd:cd06194 39 ARSYSPTSLPDG-DNELEFHIRRK-----------PNGAFSGWLgEEARPGHALR--LQGpfGQAFYRPEYGEGPLLLVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 918 PGTGIAPFRSFWQQrQFDIQHKGmnpcPMVLVFGCRQskIDHIYREETLQ--AKNKGVFRelYTAYSREPDKPKkyvQDI 995
Cdd:cd06194 105 AGTGLAPLWGIARA-ALRQGHQG----EIRLVHGARD--PDDLYLHPALLwlAREHPNFR--YIPCVSEGSQGD---PRV 172
|
170 180
....*....|....*....|....*...
gi 323635434 996 LQEQLAESVYRALKEQggHIYVCGDVTM 1023
Cdd:cd06194 173 RAGRIAAHLPPLTRDD--VVYLCGAPSM 198
|
|
| FNR_iron_sulfur_binding_1 |
cd06215 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
842-1064 |
1.03e-04 |
|
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.
Pssm-ID: 99811 [Multi-domain] Cd Length: 231 Bit Score: 44.89 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 842 RYYSISSSPDMyPDEVHLTVAivsyRTRDGEGpihhgvcSSWLNriqaDELVPcfvrG------APS--FHLPRNPQVPC 913
Cdd:cd06215 47 RAYTLSSSPSR-PDSLSITVK----RVPGGLV-------SNWLH----DNLKV----GdelwasGPAgeFTLIDHPADKL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 914 ILVGPGTGIAPFRS---FWQQRQFDIQhkgmnpcpMVLVFGCRqSKIDHIYREE--TLQAKNKGvFRELYTAYSREPDKP 988
Cdd:cd06215 107 LLLSAGSGITPMMSmarWLLDTRPDAD--------IVFIHSAR-SPADIIFADEleELARRHPN-FRLHLILEQPAPGAW 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 323635434 989 KKYVQDILQEQLAeSVYRALKEQggHIYVCGDVTMAADVlkaiqrimtqqgKLSAEDAGVfisrmrDDNRYHEDIF 1064
Cdd:cd06215 177 GGYRGRLNAELLA-LLVPDLKER--TVFVCGPAGFMKAV------------KSLLAELGF------PMSRFHQESF 231
|
|
| FldA |
COG0716 |
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ... |
424-490 |
1.12e-04 |
|
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440480 [Multi-domain] Cd Length: 135 Bit Score: 43.35 E-value: 1.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 323635434 424 ATILYATETGKSQAYAKTLCEIFKhAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGnGDPPENGEKF 490
Cdd:COG0716 1 ILIVYGSTTGNTEKVAEAIAEALG-AAGVDLFEIEDADLDDLEDYDLLILGTPTWA-GELPDDWEDF 65
|
|
| phenol_2-monooxygenase_like |
cd06211 |
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ... |
841-1045 |
1.48e-04 |
|
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.
Pssm-ID: 99807 Cd Length: 238 Bit Score: 44.62 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 841 PRYYSISSSPDMyPDEVHLTVAIVsyrtrdgEGpihhGVCSSWLNRI--QADELVpcFVRGAPSFHLPRNPQVPCILVGP 918
Cdd:cd06211 52 TRAFSIASSPSD-AGEIELHIRLV-------PG----GIATTYVHKQlkEGDELE--ISGPYGDFFVRDSDQRPIIFIAG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 919 GTGIAPFRSFWqqrqFDIQHKGMnPCPMVLVFGCRqSKIDHIYREETLQ-AKNKGVFRELyTAYSREPDKP-----KKYV 992
Cdd:cd06211 118 GSGLSSPRSMI----LDLLERGD-TRKITLFFGAR-TRAELYYLDEFEAlEKDHPNFKYV-PALSREPPESnwkgfTGFV 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 323635434 993 QDILQeqlaesvyRALKEQG-GH-IYVCGDVTMaadVLKAIQRIMtqQGKLSAED 1045
Cdd:cd06211 191 HDAAK--------KHFKNDFrGHkAYLCGPPPM---IDACIKTLM--QGRLFERD 232
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
844-1033 |
6.74e-04 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 43.34 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 844 YSISSSPDMyPDEVHLTVAIVsyrtrdgegpihhGVCSSWLNRIQADELVpcFVRGaP--SFHLPRNPQVPC-ILVGPGT 920
Cdd:COG4097 266 FSISSAPGG-DGRLRFTIKAL-------------GDFTRRLGRLKPGTRV--YVEG-PygRFTFDRRDTAPRqVWIAGGI 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 921 GIAPFRSFWQqrqfDIQHKGMNPCPMVLVFGCRQSKiDHIYREE--TLQAKNKGVfrELYTAYSREPDKpkkyvqdILQE 998
Cdd:COG4097 329 GITPFLALLR----ALAARPGDQRPVDLFYCVRDEE-DAPFLEElrALAARLAGL--RLHLVVSDEDGR-------LTAE 394
|
170 180 190
....*....|....*....|....*....|....*
gi 323635434 999 QLAESVyRALKEQggHIYVCGDVTMAADVLKAIQR 1033
Cdd:COG4097 395 RLRRLV-PDLAEA--DVFFCGPPGMMDALRRDLRA 426
|
|
| flavohem_like_fad_nad_binding |
cd06184 |
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
841-1065 |
9.07e-04 |
|
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.
Pssm-ID: 99781 Cd Length: 247 Bit Score: 42.16 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 841 PRYYSISSspdmYPDEVHLTVAIvsyrTRDgegpiHHGVCSSWL-NRIQA-DEL---VPCfvrGapSFHLPRNPQVPCIL 915
Cdd:cd06184 57 IRQYSLSD----APNGDYYRISV----KRE-----PGGLVSNYLhDNVKVgDVLevsAPA---G--DFVLDEASDRPLVL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 916 VGPGTGIAPFRSFwqqrqfdIQH--KGMNPCPMVLVFGCRQSKiDHIYREET--LQAKNKGVfrELYTAYSrEPDKPKKY 991
Cdd:cd06184 119 ISAGVGITPMLSM-------LEAlaAEGPGRPVTFIHAARNSA-VHAFRDELeeLAARLPNL--KLHVFYS-EPEAGDRE 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 323635434 992 VQDILQEQL-AESVYRALKEQGGHIYVCGDVTMAADVLKAIQrimtqqgklsaeDAGVfisrmrDDNRYHEDIFG 1065
Cdd:cd06184 188 EDYDHAGRIdLALLRELLLPADADFYLCGPVPFMQAVREGLK------------ALGV------PAERIHYEVFG 244
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
842-1030 |
3.27e-03 |
|
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.
Pssm-ID: 99786 [Multi-domain] Cd Length: 224 Bit Score: 40.22 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 842 RYYSISSSPDMYPD-EVHLtvaivsyrtRDGEGpihhGVCSS-WLNRIQADELVPcfVRGaP--SFHLPRNPQVPCILVG 917
Cdd:cd06189 42 RPFSIASAPHEDGEiELHI---------RAVPG----GSFSDyVFEELKENGLVR--IEG-PlgDFFLREDSDRPLILIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635434 918 PGTGIAPFRSFWQqrqfDIQHKGMNPcPMVLVFGCRQSKiDHIYRE--ETLQAKNKGVFrelYTA-YSREPDKPKK---Y 991
Cdd:cd06189 106 GGTGFAPIKSILE----HLLAQGSKR-PIHLYWGARTEE-DLYLDEllEAWAEAHPNFT---YVPvLSEPEEGWQGrtgL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 323635434 992 VQDILQEQLAEsvyraLKEQggHIYVCGDVTMAADVLKA 1030
Cdd:cd06189 177 VHEAVLEDFPD-----LSDF--DVYACGSPEMVYAARDD 208
|
|
| |
