|
Name |
Accession |
Description |
Interval |
E-value |
| chlB |
CHL00076 |
photochlorophyllide reductase subunit B |
1-505 |
0e+00 |
|
photochlorophyllide reductase subunit B
Pssm-ID: 214355 [Multi-domain] Cd Length: 513 Bit Score: 781.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 1 MKLAYWMYAGPAHIGTLRIASSFQNVLAIMHAPLGDDYFNVMRSMLERQKNLPKVTTNIIDRHVLTQGSANKIIRNIIRK 80
Cdd:CHL00076 1 MKLAYWMYAGPAHIGTLRVASSFKNVHAIMHAPLGDDYFNVMRSMLERERDFTPVTASIVDRHVLARGSQEKVVDNITRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 81 DKEESPKLILITPTCTSSILQEDLDNFIKKSSLETNADVLLADINHYRNNEYQAADITLKQIIHFYI---KKYTNSKISL 157
Cdd:CHL00076 81 DKEERPDLIVLTPTCTSSILQEDLQNFVDRASIESDSDVILADVNHYRVNELQAADRTLEQIVRFYLekaRKQGTLDQSK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 158 TKEPSVNIIGAYSLAFHNQHDILELIKVLTELNIKINLILPKGASIEELEKLPKAWVNIVPYRETGILAAKWLKENFNIP 237
Cdd:CHL00076 161 TDKPSVNIIGIFTLGFHNQHDCRELKRLLQDLGIEINQIIPEGGSVEDLKNLPKAWFNIVPYREVGLMTAKYLEKEFGMP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 238 YISTTPLGHENLAIWIKELEYCLKSKGRVNL----NFNNFIENKTTFNSQSFWFSRSIDCQNLIGKSAVVFGDSTHVAAI 313
Cdd:CHL00076 241 YISTTPMGIVDTAECIRQIQKILNKLASDILekkvDYEKYIDQQTRFVSQAAWFSRSIDCQNLTGKKAVVFGDATHAASM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 314 TKILKKDLGINILWAGTYCISDQNWFKHTLKEYTNNIFVSENYSVVEKLIKIASPDAIFGTQMERHVGKKLGIPCGVISA 393
Cdd:CHL00076 321 TKILAREMGIRVSCAGTYCKHDAEWFKEQVQGFCDEILITDDHTEVGDMIARVEPSAIFGTQMERHIGKRLDIPCGVISA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 394 PIHIQNYPIGYRPFFGYEGANQLIDMIYNTFSLGMETILLEVFGGHDRQVTETASFLNKGDIYWTKEAENIFAQIPKIFQ 473
Cdd:CHL00076 401 PVHIQNFPLGYRPFLGYEGTNQIADLVYNSFTLGMEDHLLEIFGGHDTKEIITKSLSTDSDLIWSPESQLELSKIPGFVR 480
|
490 500 510
....*....|....*....|....*....|..
gi 1833819266 474 KKIKHKIDTYAASLNKTIVTPEILYKAKASLT 505
Cdd:CHL00076 481 GKVKRNTEKFARQNGITNITVEVMYAAKEALS 512
|
|
| BchB |
COG5746 |
Light-independent protochlorophyllide reductase subunit B, BchB (= ChlB) [Coenzyme transport ... |
1-504 |
0e+00 |
|
Light-independent protochlorophyllide reductase subunit B, BchB (= ChlB) [Coenzyme transport and metabolism];
Pssm-ID: 444456 [Multi-domain] Cd Length: 536 Bit Score: 631.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 1 MKLAYWMYAGPAHIGTLRIASSFQNVLAIMHAPLGDDYFNVMRSMLERQKNLPKVTTNIIDRHVLTQGSANKIIRNIIRK 80
Cdd:COG5746 1 MRLAYWTYEGPAHIGAMRVATSMKGVHYVLHAPQGDDYADLLFTMLERRPDFPPVTYSTVQARDLGRGTAELVKDTIRQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 81 DKEESPKLILITPTCTSSILQEDLDNFIKKSSLetNADVLLADINHYRNNEYQAADITLKQIIHFYIKKYTNSKISLTKE 160
Cdd:COG5746 81 DERFKPDLIVVGPSCTAELLQEDLGGLARRAGL--PIPVLLLDLNAYRVKENWGADETFYQLVRFLAKPAGRLPQEKTER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 161 PSVNIIGAYSLAFHNQHDILELIKVLTELNIKINLILPKGASIEELEKLPKAWVNIVPYRETGILAAKWLKENFNIPYIS 240
Cdd:COG5746 159 PSVNILGPTSLGFHHRDDLTELTRLLATLGIEVNVVAPLGASPADLARLPAAWFNVVPYREIGLGAARYLERTFGQPYTK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 241 TTPLGHENLAIWIKELEYCLKSKGRvNLNFNNFIENKTTFNSQSFWFSRSIDCQNLIGKSAVVFGDSTHVAAITKILKKD 320
Cdd:COG5746 239 TVPIGVGATARFIREVQQLLNVQGA-DPPLEAFSPDGTSAPSRVPWFSRSVDSTYLTGKRAFVFGDATHAVAAARILRDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 321 LGINILWAGTYCISDQNWFKHTLKEYTNNIFVSENYSVVEKLIKIASPDAIFGTQMERHVGKKLGIPCGVISAPIHIQNY 400
Cdd:COG5746 318 LGFEVVGAGTYSREFARWVRAEAAGYGDEALITDDYLEVEAAIAELEPELVLGTQMERHSAKRLGIPCAVISAPVHVQDF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 401 PIGYRPFFGYEGANQLIDMIYNTFSLGMETILLEVFGG----HD------------------RQVTETASFLNK------ 452
Cdd:COG5746 398 PARYSPFMGFEGANVIFDTVYHPLTLGLEEHLLDMFGGdfefHDtagpshlgaaapepaaasAAEGAPAAEPATeaitap 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1833819266 453 -----GDIYWTKEAENIFAQIPKIFQKKIKHKIDTYAASLNKTIVTPEILYKAKASL 504
Cdd:COG5746 478 aasapGDPVWTADAEAELKKIPFFVRGKVRRNTEKYARERGLTEITAEVLYAAKEHL 534
|
|
| PRK02910 |
PRK02910 |
ferredoxin:protochlorophyllide reductase (ATP-dependent) subunit B; |
1-504 |
0e+00 |
|
ferredoxin:protochlorophyllide reductase (ATP-dependent) subunit B;
Pssm-ID: 235085 [Multi-domain] Cd Length: 519 Bit Score: 625.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 1 MKLAYWMYAGPAHIGTLRIASSFQNVLAIMHAPLGDDYFNVMRSMLERQKNLPKVTTNIIDRHVLTQGSANKIIRNIIRK 80
Cdd:PRK02910 1 MRLAYWTYEGPAHVGAMRIATSMKGVHYVLHAPQGDDYADLLFTMLERRGKRPPVTYSTVQARDLARGTAELLKDTLRRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 81 DKEESPKLILITPTCTSSILQEDLDNFIKksSLETNADVLLADINHYRNNEYQAADITLKQIIHFYIKKYTNSKISLTKE 160
Cdd:PRK02910 81 DERFQPDLIVVGPSCTAELLQEDLGGLAK--HAGLPIPVLPLELNAYRVKENWAADETFYQLVRALAKKAAELPQPKTAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 161 PSVNIIGAYSLAFHNQHDILELIKVLTELNIKINLILPKGASIEELEKLPKAWVNIVPYRETGILAAKWLKENFNIPYIS 240
Cdd:PRK02910 159 PSVNLLGPTALGFHHRDDLTELRRLLATLGIDVNVVAPLGASPADLKRLPAAWFNVVLYREIGESAARYLEREFGQPYVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 241 TTPLGHENLAIWIKELEYCLKSKGRvnlNFNNFIENKTTFNSQSFWFSRSIDCQNLIGKSAVVFGDSTHVAAITKILKKD 320
Cdd:PRK02910 239 TVPIGVGATARFIREVAELLNLDGA---DLEAFILDGLSAPSRLPWFSRSVDSTYLTGKRVFVFGDATHAVAAARILSDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 321 LGINILWAGTYCISDQNWFKHTLKEYTNNIFVSENYSVVEKLIKIASPDAIFGTQMERHVGKKLGIPCGVISAPIHIQNY 400
Cdd:PRK02910 316 LGFEVVGAGTYLREDARWVRAAAKEYGDEALITDDYLEVEDAIAEAAPELVLGTQMERHSAKRLGIPCAVISAPTHVQDF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 401 PIGYRPFFGYEGANQLIDMIYNTFSLGMETILLEVFG------------------GHDRQVTETASFLNKGDIYWTKEAE 462
Cdd:PRK02910 396 PARYSPQMGFEGANVIFDTWYHPLMLGLEEHLLDMFGddfefydgaaaaaaaasaGHDTKEVATKAAAADSELVWTPEAE 475
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1833819266 463 NIFAQIPKIFQKKIKHKIDTYAASLNKTIVTPEILYKAKASL 504
Cdd:PRK02910 476 AELKKIPFFVRGKVRRNTEKFARERGLPEITLEVLYDAKAHF 517
|
|
| DPOR_BchB |
TIGR01278 |
light-independent protochlorophyllide reductase, B subunit; Alternate name: dark ... |
1-504 |
0e+00 |
|
light-independent protochlorophyllide reductase, B subunit; Alternate name: dark protochlorophyllide reductase This enzyme describes the B subunit of the dark form protochlorophyllide reductase, a nitrogenase-like enzyme. This subunit shows homology to the nitrogenase molybdenum-iron protein. It catalyzes a step in bacteriochlorophyll biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273534 [Multi-domain] Cd Length: 511 Bit Score: 623.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 1 MKLAYWMYAGPAHIGTLRIASSFQNVLAIMHAPLGDDYFNVMRSMLERQKNLPKVTTNIIDRHVLTQGSANKIIRNIIRK 80
Cdd:TIGR01278 1 MKLAYWMYEGPAHIGVLRIASSMKNVHAVMHAPQGDDYVNVMFSMLERTPNFPPVTTSVVDRRDLARGSQTRLVDTVRRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 81 DKEESPKLILITPTCTSSILQEDLDNFIKKSSLEtNADVLLADINHYRNNEYQAADITLKQIIHFYIKKyTNSKISLTKE 160
Cdd:TIGR01278 81 DDRFKPDLIVVTPSCTSSLLQEDLGNLAAAAGLD-KSKVIVADVNAYRRKENQAADRTLTQLVRRFAKE-QPKPGRTTEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 161 PSVNIIGAYSLAFHNQHDILELIKVLTELNIKINLILPKGASIEELEKLPKAWVNIVPYRETGILAAKWLKENFNIPYIS 240
Cdd:TIGR01278 159 PSVNLLGPASLGFHHRHDLIELRRLLKTLGIEVNVVAPWGASIADLARLPAAWLNICPYREIGLMAAEYLKEKFGQPYIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 241 TTPLGHENLAIWIKELEYCLKSKGrVNLNFNNFIENKTTFNSQSFWFSRSIDCQNLIGKSAVVFGDSTHVAAITKILKKD 320
Cdd:TIGR01278 239 TTPIGVNATRRFIREIAALLNQAG-ADPYYESFILDGLSAVSQAAWFARSIDSQSLTGKRAFVFGDATHAVGMTKILARE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 321 LGINILWAGTYCISDQNWFKHTLKEYTNNIFVSENYSVVEKLIKIASPDAIFGTQMERHVGKKLGIPCGVISAPIHIQNY 400
Cdd:TIGR01278 318 LGIHIVGAGTYCKYDADWVREQVAGYVDEVLITDDFQEVADAIAALEPELVLGTQMERHSAKRLDIPCGVISAPTHIQNF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 401 PIGYRPFFGYEGANQLIDMIYNTFSLGMETILLEVFG--GHD-RQVTETA------SFLNKGDIYWTKEAENIFAQIPKI 471
Cdd:TIGR01278 398 PLGYRPFLGFEGANVMADTVYNTFKLGLEEHLLEMFGdaGHDtPAHLEPAataaisSAPAPGELGWTAEAEAELKKVPFF 477
|
490 500 510
....*....|....*....|....*....|...
gi 1833819266 472 FQKKIKHKIDTYAASLNKTIVTPEILYKAKASL 504
Cdd:TIGR01278 478 VRGKVRRNTENFARERGYSVITLEVIYAAKEHF 510
|
|
| Pchlide_reductase_B |
cd01981 |
Pchlide_reductase_B: B protein of the NB protein complex of Protochlorophyllide (Pchlide) ... |
1-427 |
0e+00 |
|
Pchlide_reductase_B: B protein of the NB protein complex of Protochlorophyllide (Pchlide)_reductase. Pchlide reductase catalyzes the reductive formation of chlorophyllide (chlide) from protochlorophyllide (pchlide) during biosynthesis of chlorophylls and bacteriochlorophylls. This group contains both the light-independent Pchlide reductase (DPOR) and light-dependent Pchlide reductase (LPOR). Angiosperms contain only LPOR, cyanobacteria, algae and gymnosperms contain both DPOR and LPOR, primitive anoxygenic photosynthetic bacteria contain only DPOR. NB is structurally similar to the FeMo protein of nitrogenase, forming an N2B2 heterotetramer. N and B are homologous to the FeMo alpha and beta subunits respectively. Also in common with nitrogenase in vitro DPOR activity requires ATP hydrolysis and dithoionite or ferredoxin as electron donor. The NB protein complex may serve as a catalytic site for Pchlide reduction similar to MoFe for nitrogen reduction.
Pssm-ID: 238939 [Multi-domain] Cd Length: 430 Bit Score: 620.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 1 MKLAYWMYAGPAHIGTLRIASSFQNVLAIMHAPLGDDYFNVMRSMLERQKNLPKVTTNIIDRHVLTQGSANKIIRNIIRK 80
Cdd:cd01981 1 MKLAYWMYEGPAHIGTLRVASSFKNVHAVMHAPLGDDYFNVMRSMLERERDFTPVTASTVDRHVLARGSQEKVVENITRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 81 DKEESPKLILITPTCTSSILQEDLDNFIKKSSLETNADVLLADINHYRNNEYQAADITLKQIIHFYIKK--YTNSKISLT 158
Cdd:cd01981 81 DKEEKPDLIVLTPTCTSSILQEDLQNFVRAAGLSSKSPVLPLDVNHYRVNELQAADETFEQLVRFYAEKarPQGTPREKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 159 KEPSVNIIGAYSLAFHNQHDILELIKVLTELNIKINLILPKGASIEELEKLPKAWVNIVPYRETGILAAKWLKENFNIPY 238
Cdd:cd01981 161 EKPSVNLIGPSSLGFHNRHDCRELKRLLHTLGIEVNVVIPEGASVDDLNELPKAWFNIVPYREYGLSAALYLEEEFGMPS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 239 ISTTPLGHENLAIWIKELEYCLKSKGR-VNLNFNNFIENKTTFNSQSFWFSRSIDCQNLIGKSAVVFGDSTHVAAITKIL 317
Cdd:cd01981 241 VKITPIGVVATARFLREIQELLGIQIIpELVNVEPYIDSQTRWVSQSARSSRSIDSQNLTGKRAFVFGDATHVAAATRIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 318 KKDLGINILWAGTYCISDQNWFKHTLKEYTNNIFVSENYSVVEKLIKIASPDAIFGTQMERHVGKKLGIPCGVISAPIHI 397
Cdd:cd01981 321 AREMGFRVVGAGTYCKEDAKWFREQATGYCDEALITDDHTEVGDMIARTEPELIFGTQMERHIGKRLDIPCAVISAPVHI 400
|
410 420 430
....*....|....*....|....*....|
gi 1833819266 398 QNYPIGYRPFFGYEGANQLIDMIYNTFSLG 427
Cdd:cd01981 401 QNFPLGYRPFLGYEGTNVIADTVYNSLTLG 430
|
|
| Oxidoreductase_nitrogenase |
cd00316 |
The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. ... |
5-424 |
4.48e-104 |
|
The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. This group contains both alpha and beta subunits of component 1 of the three known genetically distinct types of nitrogenase systems: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium-dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase) and, both subunits of Protochlorophyllide (Pchlide) reductase and chlorophyllide (chlide) reductase. The nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). The most widespread and best characterized nitrogenase is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers whose alpha and beta subunits are similar to the alpha and beta subunits of MoFe. For MoFe, each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains a single [4Fe-4S] cluster from which, electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo at the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. Pchlide reductase and chlide reductase participate in the Mg-branch of the tetrapyrrole biosynthetic pathway. Pchlide reductase catalyzes the reduction of the D-ring of Pchlide during the synthesis of chlorophylls (Chl) and bacteriochlorophylls (BChl). Chlide-a reductase catalyzes the reduction of the B-ring of Chlide-a during the synthesis of BChl-a. The Pchlide reductase NB complex is a an N2B2 heterotetramer resembling nitrogenase FeMo, N and B proteins are homologous to the FeMo alpha and beta subunits respectively. The NB complex may serve as a catalytic site for Pchlide reduction and, the ZY complex as a site of chlide reduction, similar to MoFe for nitrogen reduction.
Pssm-ID: 238193 [Multi-domain] Cd Length: 399 Bit Score: 316.91 E-value: 4.48e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 5 YWMYAGPAHIGTLRIASSFQNVLAIMHAPLGDDYFNVMRSMLERQKNLPKVTTNIIDRHVLtQGSANKIIRNIIRKDKEE 84
Cdd:cd00316 1 INPAKGCAPLGAARVALGIKDAIPLVHGPQGCAYFTRLTLRRHFKEPIPLFTTSMTEKDVV-FGGGEKLLEAIINELKRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 85 SPKLILITPTCTSSILQEDLDNFIKKSSLETNADVLLADINHYRNNEYQAADITLKQIIHFYIKKYTNSKislTKEPSVN 164
Cdd:cd00316 80 KPKVIFVYTTCTTELIGDDIEAVAKEASKEIGIPVVPASTPGFRGSQSAGYDAAVKAIIDHLVGTAEPEE---TEPGSVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 165 IIGAYSLAFHnqhDILELIKVLTELNIKINLILPKGASIEELEKLPKAWVNIVPYRETGILAAKWLKENFNIPYISTTPL 244
Cdd:cd00316 157 LIGGYNLGGG---DLRELKRLLEEMGIRVNALFDGGTTVEELRELGNAKLNLVLCRESGLYLARYLEEKYGIPYILINPI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 245 GHENLAIWIKEL-EYCLKSKgrvnlNFNNFIENKTTFNSQSFWFSRsidcQNLIGKSAVVFGDSTHVAAITKILkKDLGI 323
Cdd:cd00316 234 GLEATDAFLRKLaELFGIEK-----EVPEVIARERARLLDALADYH----EYLGGKKVAIFGDGDLLLALARFL-LELGM 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 324 NILWAGTYCISDQNWFKHTLKEYTNN-IFVSENYSVVEKLIKIASPDAIFGTQMERHVGKKLGIPCGVISAPIHiqnypi 402
Cdd:cd00316 304 EVVAAGTTFGHKADYERREELLGEGTeVVDDGDLEELEELIRELKPDLIIGGSKGRYIAKKLGIPLVRIGFPIH------ 377
|
410 420
....*....|....*....|..
gi 1833819266 403 gYRPFFGYEGANQLIDMIYNTF 424
Cdd:cd00316 378 -RRPYVGYEGALNLAEEIANAL 398
|
|
| Oxidored_nitro |
pfam00148 |
Nitrogenase component 1 type Oxidoreductase; |
12-424 |
5.17e-71 |
|
Nitrogenase component 1 type Oxidoreductase;
Pssm-ID: 395096 [Multi-domain] Cd Length: 398 Bit Score: 231.37 E-value: 5.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 12 AHIGTLRIASSFQNVLAIMHAPLG-DDYFNVMRSMLERqKNLPKVTTNIIDRHVLTQGSAN--KIIRNIIRKDKeesPKL 88
Cdd:pfam00148 2 APAGASVALLGIKDAVPLVHGPQGcATYVRLLLTRHFR-EPIPLATTSLTEKDVVFGGEENlkEAIKEVDKRYK---PKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 89 ILITPTCTSSILQEDLDNFIKKSSLETNADVLLADINHYRNNEYQAADITLKQIIHFYIKKytnskiSLTKEP-SVNIIG 167
Cdd:pfam00148 78 IFVISTCLTETIGDDIEAVAREAREELGIPVIPVSTPGFVGSHSTGYDVALEAIVRQLVGK------KGEKEPgTVNILG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 168 AYSLAFHnqhDILELIKVLTELNIKINLILPKGASIEELEKLPKAWVNIVPYRETGILAAKWLKENFNIPYIS-TTPLGH 246
Cdd:pfam00148 152 GFNLGPG---DLREIKRLLEKLGIEVNPVFTGGTTLEDLRAAGNAAANLVLCPFSGEYAAEMLEEKFGVPYIRlGAPIGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 247 ENLAIWIKELEYCLKsKGRVNlnfNNFIENKTTfnsqsfWFSRSIDCQN-LIGKSAVVFGDSTHVAAITKILkKDLGINI 325
Cdd:pfam00148 229 EATDRFLRALAKLFG-KEVAP---EVIARERGR------LLDAMVDYHEyLAGKRVAIYGDPDLVLGLARFL-LELGMEP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 326 LWAGTYCIS--DQNWFKHTLKEYTNNIFVSENYSVVEKLIKIASPDAIFGTQMERHVGKKLGIPCGVISAPIHIQNYPIg 403
Cdd:pfam00148 298 VAVGTGTGHpdDYERLKAELEEGDPEVIDGADLEELEELIKELKPDLLLGNSKGRYIARKLGIPLVRVGFPIVDRHGLH- 376
|
410 420
....*....|....*....|.
gi 1833819266 404 YRPFFGYEGANQLIDMIYNTF 424
Cdd:pfam00148 377 RRPYVGYRGALNLADRIANAL 397
|
|
| NifD/CfbD |
COG2710 |
Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and ... |
14-424 |
3.60e-31 |
|
Nitrogenase Mo-Fe protein NifD/coenzyme F430 biosynthesis subunit CfbD [Coenzyme transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 442027 [Multi-domain] Cd Length: 416 Bit Score: 124.84 E-value: 3.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 14 IGTLRIASSFQNVLAIMHAPLGDDYFnvMRSMLERQKNLPK--VTTNIIDRHVLTQGSAN--KIIRNIIRKDKeesPKLI 89
Cdd:COG2710 16 LGAKLALLGIKDAIPLVHGSQGCAAY--SRVTRGRHFKEPIplFSTDMTEDDVVFGGEKNleEAIKNIIERYK---PKLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 90 LITPTCTSSILQEDLDNFIKKSSLETNADVLLADINHYRNNEYQAADITLKQIIHFYIKKYtnskiSLTKEPSVNIIGAY 169
Cdd:COG2710 91 FVYTTCLTETIGDDIEAVIKEAREELGIPVVPVSTPGFVGSHSTGYHIAVEAIVEQLVGTG-----EPKTPGKINLIGGY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 170 SLafhNQHDILELIKVLTELNIKINLILPKG-ASIEELEKLPKAWVNIVPYRETGILAAKWLKENFNIPYIST-TPLGHE 247
Cdd:COG2710 166 NL---IPGDLWEIKRLLEEMGLRVIALPDLGgTTVEEIADAGRAKLNLVLCSRSGNYAARYLEEKYGIPYLEFvSPIGLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 248 NLAIWIKELEYCLKSKGRvnlnfnNFIENKTtfnsqsfwfSRSIDC-----QNLIGKSAVVFGDSTHVAAITKILkKDLG 322
Cdd:COG2710 243 ATDEFLRKLAELFGKPVP------EVIARER---------GRLVDAladyhFYLGGKKVAIYGDPDLLWGLASFL-LELG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 323 INILWAGTYciSDQNWFKHTLKEYTNN-----IFVSENYSVVEKLIKIASPDAIFGTQMERHVGKKLGIPCGVISAPIHI 397
Cdd:COG2710 307 MEPVAAVTT--TGSPEDYERIKELLEElpegtVIDDGDLEELEELLKELKPDLLIGGSKGKYLARKLGIPLLRVGFPIYD 384
|
410 420
....*....|....*....|....*..
gi 1833819266 398 QNYpIGYRPFFGYEGANQLIDMIYNTF 424
Cdd:COG2710 385 RVG-LQRRPYAGYRGALNLLEDIANAL 410
|
|
| Nitrogenase_VnfN_like |
cd01971 |
Nitrogenase_vnfN_like: VnfN subunit of the VnfEN complex-like. This group in addition to VnfN ... |
15-423 |
7.35e-29 |
|
Nitrogenase_vnfN_like: VnfN subunit of the VnfEN complex-like. This group in addition to VnfN contains a subset of the beta subunit of the nitrogenase MoFe protein and NifN-like proteins. The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of MoFe protein of the molybdenum(Mo)-nitrogenase. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to NifEN where it is further processed to FeMoco. VnfEN may similarly be a scaffolding protien for the iron-vanadium cofactor (FeVco) of the vanadium-dependent (V)-nitrogenase. NifE and NifN are essential for the Mo-nitrogenase, VnfE and VnfN are not essential for the V-nitrogenase. NifE and NifN can substitute when the vnfEN genes are inactivated.
Pssm-ID: 238931 [Multi-domain] Cd Length: 427 Bit Score: 118.29 E-value: 7.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 15 GTLRIASSFQNVLAIMHAPLG---DDYFNVMRSMLERQKNLPKV-TTNIIDRHVLTQGSaNKIiRNIIRKDKEESP-KLI 89
Cdd:cd01971 13 GALYTVSAIPRAVPIIHSGPGcasKQSGAVAFGNGYQGGGYGVApCTNATETEIVFGGE-DRL-RELIKSTLSIIDaDLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 90 LITPTCTSSILQEDLDNFIKKSSlETNADVLLADINHYRNNEYQAADITLKQIIHFYIKKYTNSKISLtkepsVNIIG-- 167
Cdd:cd01971 91 VVLTGCIAEIIGDDVGAVVSEFQ-EGGAPIVYLETGGFKGNNYAGHEIVLKAIIDQYVGQSEEKEPGL-----VNLWGpv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 168 AYSLAFHNQhDILELIKVLTELNIKINLILPKGASIEELEKLPKAWVNIVPYRETGILAAKWLKENFNIPYI--STTPLG 245
Cdd:cd01971 165 PYQDPFWRG-DLEEIKRVLEGIGLKVNILFGPESNGEELRSIPKAQFNLVLSPWVGLEFAQHLEEKYGQPYIhsPTLPIG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 246 HENLAIWIKELeycLKSKGRVNLNFNNFI--ENKTT---FNSQSFWFSRsidcQNLIGKSAVVfGDSTHVAAITKILKKD 320
Cdd:cd01971 244 AKATAEFLRQV---AKFAGIEKAKVEAFIkaEEKRYyhyLERFSDFMAR----WGLPRRFAVI-ADSTYALGLARFLVNE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 321 LGINilwAGTYCISDQNWFKHTL---KEYTNN------IFVSENYSVVEKLIK---IASPDAIFGTQMERHVGKKLGIPC 388
Cdd:cd01971 316 LGWV---PAKQVITDNPPEKYRSaieNEFEAEgvsaevVFSEDGYAIGQSLRQsdfKYKPPIIFGSSWERDLAKELGGKI 392
|
410 420 430
....*....|....*....|....*....|....*.
gi 1833819266 389 GVISAPIhiqNYPIGY-RPFFGYEGANQLIDMIYNT 423
Cdd:cd01971 393 LEVSFPV---TNRVVLnRGYAGYRGALTLLEDIYTT 425
|
|
| Nitrogenase_MoFe_beta_like |
cd01965 |
Nitrogenase_MoFe_beta_like: Nitrogenase MoFe protein, beta subunit_like. The nitrogenase ... |
14-424 |
4.14e-25 |
|
Nitrogenase_MoFe_beta_like: Nitrogenase MoFe protein, beta subunit_like. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen (N2) to ammonia. This group contains the beta subunits of component 1 of the three known genetically distinct types of nitrogenase systems: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium-dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase). These nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). The most widespread and best characterized of these systems is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers having alpha and beta subunits similar to the alpha and beta subunits of MoFe. For MoFe, each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains, a single [4Fe-4S] cluster from which electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo, the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo-nitrogenase in that it produces free hydrazine, as a minor product during N2-reduction and, ethane as a minor product during acetylene reduction
Pssm-ID: 238927 [Multi-domain] Cd Length: 428 Bit Score: 107.27 E-value: 4.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 14 IGTLRIASSFQNVLAIMHAPLG-DDYFnvmRSMLER--QKNLPKVTTNIIDRHVLTQGSANKI--IRNIIRKDKeesPKL 88
Cdd:cd01965 11 LGAALAFLGIEGCMPLVHGSQGcSSFA---RVLFTRhfKEPIPIASTSMTEDAAVFGGEDNLIeaLKNLLSRYK---PDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 89 ILITPTCTSSILQEDLDNFIK--KSSLETNADVLLADIN--HYRNNEYQAADITLKQIIHFYIKKYtnskiSLTKEPSVN 164
Cdd:cd01965 85 IGVLTTCLTETIGDDVAGFIKefRAEGPEPADFPVVYAStpSFKGSHETGYDNAVKAIIEQLAKPS-----EVKKNGKVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 165 IIGAyslaFHNQHDILELIK-VLTELNIKINlILP-------------------KGASIEELEKLPKAWVNIVPYRETGI 224
Cdd:cd01965 160 LLPG----FPLTPGDVREIKrILEAFGLEPI-ILPdlsdsldghltdgyspltkGGTTLEEIRDAGNAKATIALGEYSGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 225 LAAKWLKENFNIPYI-STTPLGHENLAIWIKELeyclkSKgrvnlnfnnfIENKTTFNSQSFWFSRSID-----CQNLIG 298
Cdd:cd01965 235 KAAKALEEKFGVPYIlFPTPIGLKATDEFLRAL-----SK----------LSGKPIPEELERERGRLLDamldsHFYLGG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 299 KSAVVFGDSTHVAAITKILkKDLGINILWAgtYCISDQNWFKHTLKEYTN------NIFVSENYSVVEKLIKIASPDAIF 372
Cdd:cd01965 300 KRVAIAGDPDLLLGLSRFL-LEMGAEPVAA--VTGTDNPPFEKRMELLASlegipaEVVFVGDLWDLESLAKEEPVDLLI 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1833819266 373 GTQMERHVGKKLGIPCGVISAPIHiqnYPIGY--RPFFGYEGANQLIDMIYNTF 424
Cdd:cd01965 377 GNSHGRYLARDLGIPLVRVGFPIF---DRLGLhrRPYVGYRGALNLLEEIANTL 427
|
|
| Nitrogenase_VnfE_like |
cd01972 |
Nitrogenase_VnfE_like: VnfE subunit of the VnfEN complex_like. This group in addition to VnfE ... |
19-413 |
4.51e-25 |
|
Nitrogenase_VnfE_like: VnfE subunit of the VnfEN complex_like. This group in addition to VnfE contains a subset of the alpha subunit of the nitrogenase MoFe protein and NifE-like proteins. The nitrogenase enzyme system catalyzes the ATP-dependent reduction of dinitrogen to ammonia. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of MoFe protein of the molybdenum(Mo)-nitrogenase. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to NifEN where it is further processed to FeMoco. VnfEN may similarly be a scaffolding protein for the iron-vanadium cofactor (FeVco) of the vanadium-dependent (V)-nitrogenase. NifE and NifN are essential for the Mo-nitrogenase, VnfE and VnfN are not essential for the V-nitrogenase. NifE and NifN can substitute when the vnfEN genes are inactivated.
Pssm-ID: 238932 [Multi-domain] Cd Length: 426 Bit Score: 107.51 E-value: 4.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 19 IASSFQNVLAIMHAPLGDDY----FNVMRSMLE--RQKNLPKVTTNIIDRHVLTqGSANKIIRNIIRKDKEESPKLILIT 92
Cdd:cd01972 18 ILSGIRDAVVVQHGPIGCAAgqsfFNRLYRCGEmrRGLNEPVLSTNLTEKDVVF-GGEKKLEDTIKEAYSRYKPKAIFVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 93 PTCTSSILQEDLDNFIKKSSLETNADVLLADINHYRNNEYQAA-DITLKQIIHFYIKKYTNSKisltKEPSVNIIGAY-S 170
Cdd:cd01972 97 TSCATGIIGDDVESVVEELEDEIGIPVVALHCEGFKGKHWRSGfDAAFHGILRHLVPPQDPTK----QEDSVNIIGLWgG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 171 LAFHNQHDILELIKVLTELNIKINLILPKGASIEELEKLPKAWVNIVPYRETGILAAKWLKENFNIPYISTT-PLGHENL 249
Cdd:cd01972 173 PERTEQEDVDEFKRLLNELGLRVNAIIAGGCSVEELERASEAAANVTLCLDLGYYLGAALEQRFGVPEIKAPqPYGIEAT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 250 AIWIKELEYCLKSKGRVnlnfNNFIENKTTFNSQSFWFSRsidcQNLIGKSAVVFGDSTH-VAAITKILKKDLGINIlwa 328
Cdd:cd01972 253 DKWLREIAKVLGMEAEA----EAVIEREHERVAPEIEELR----KALKGKKAIVETGAAYgHLLIAVLRELGFGEVP--- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 329 GTYC----------ISDQNWFKHTLKEYtnnIFVSeNYSV-------VEKLIKIASPDAIFgtqmERHVG------KKLG 385
Cdd:cd01972 322 VVLVfhhdptydrgDSEKDLLEHGVDPE---IDIT-KYTVsngqyyqFYNLLKRVKPDFII----FRHGGlfpdatVYLG 393
|
410 420
....*....|....*....|....*...
gi 1833819266 386 IPCGVISApihiqnypIGYRPFFGYEGA 413
Cdd:cd01972 394 IPVVPLND--------ELNQPQFGYRGL 413
|
|
| Nitrogenase_MoFe_alpha_like |
cd01967 |
Nitrogenase_MoFe_alpha_like: Nitrogenase MoFe protein, alpha subunit_like. The nitrogenase ... |
8-423 |
2.36e-24 |
|
Nitrogenase_MoFe_alpha_like: Nitrogenase MoFe protein, alpha subunit_like. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen to ammonia. Three genetically distinct types of nitrogenase systems are known to exist: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase). These nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). This group contains the alpha subunit of component 1 of all three different forms. The most widespread and best characterized of these systems is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers having alpha and beta subunits similar to the alpha and beta subunits of MoFe. The role of the delta subunit is unknown. For MoFe, each alphabeta pair of subunits contains one P-cluster (located at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein is a homodimer which contains, a single [4Fe-4S] cluster from which electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo- nitrogenase in that it produces free hydrazine, as a minor product during dinitrogen reduction and, ethane as a minor product during acetylene reduction.
Pssm-ID: 238929 [Multi-domain] Cd Length: 406 Bit Score: 104.99 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 8 YAGPAHIgtlrIASSFQNVLAIMHAPLG------DDYFNvmRSMLERQKNLPKVTTNIIDRHVLTqGSANKIIRNIIRKD 81
Cdd:cd01967 11 AFGGAGV----VLGPIKDAVHIVHGPIGcayytwDTRRN--LSSGENLFYKYGFSTDMQEKDIVF-GGEKKLKKAIKEAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 82 KEESPKLILITPTCTSSILQEDLDNFIKKSSLETNADVLLADINHYRNNEYQAA-DITLKQIIHFYIKKYTNSKislTKE 160
Cdd:cd01967 84 ERFPPKAIFVYSTCPTGLIGDDIEAVAKEASKELGIPVIPVNCEGFRGVSQSLGhHIANDAILDHLVGTKEPEE---KTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 161 PSVNIIGAYSLAfhnqHDILELIKVLTELNIKINLILPKGASIEELEKLPKAWVNIVPYRETGILAAKWLKENFNIPYIS 240
Cdd:cd01967 161 YDVNIIGEYNIG----GDAWVIKPLLEELGIRVNATFTGDGTVDELRRAHRAKLNLVHCSRSMNYLAREMEERYGIPYME 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 241 TTPLGHENLAIWIKEL-----------EYCLKSKGRVNLNFNNFIEnkttfnsqsfwfsrsidcqNLIGKSAVVF---GD 306
Cdd:cd01967 237 VNFYGFEDTSESLRKIakffgdeekaeEVIAEEEARIKPELEKYRE-------------------RLKGKKVIIYtggAR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 307 STHVAAITkilkKDLGINILWAGTycisdqnwFKHTLKEYTNNIFVSENYSVV---------EKLIKIASPDAIFGTQME 377
Cdd:cd01967 298 SWHVIAAL----RELGMEVVAAGY--------EFGHDDDYERIRKILDEGTLLvddyndlelEELVEKLKPDLILSGIKE 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1833819266 378 RHVGKKLGIPCGVISAPIHIqnypigyrPFFGYEGANQLIDMIYNT 423
Cdd:cd01967 366 KYVAQKLGIPFLDLHSERNG--------PYAGYEGFLNFARDIDTA 403
|
|
| Chlide_reductase_Z |
cd01982 |
Chlide_reductase_Z : Z subunit of chlorophyllide (chlide) reductase (BchZ). Chlide reductase ... |
4-424 |
1.42e-11 |
|
Chlide_reductase_Z : Z subunit of chlorophyllide (chlide) reductase (BchZ). Chlide reductase participates in photosynthetic pigment synthesis playing a role in the conversion of chlorophylls(Chl) into bacteriochlorophylls (BChl). Chlide reductase catalyzes the reduction of the B-ring of the tetrapyrolle. Chlide reductase is a three subunit enzyme (subunits are designated BchX, BchY and BchZ). The similarity between these three subunits and the subunits for nitrogenase suggests that BchX serves as an electron donor for the BchY-BchY catalytic subunits.
Pssm-ID: 238940 [Multi-domain] Cd Length: 412 Bit Score: 66.40 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 4 AYWmyagpahiGTLRIASSFQNVLAIMHAPLGDDYFNVMrSMLERQKNLPK----VTTNIIDRHVLTQGSANKIIRNIir 79
Cdd:cd01982 11 AYW--------GAVNTFCALKDVHVVADAPVGCYNLPGV-AVMDYTDALPYlenlTPTSLTEEEISSSGTAGAVIRTI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 80 KDKEESPKLILITPTCTSSIlqedldnfikkssletNADVLLADINHYR-------NNEYQAADITLKQIIHFY----IK 148
Cdd:cd01982 80 DKLDPSGKLILVSSAESEMI----------------GSDHTPMLTMQQPfvrffigENEWQGRDRALEWLFDEFdlrkPW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 149 KYTNSKISLTKEPSVNIIGAYSLAFHNQHDILELIKVLTELNIKINLILPKGASIEELEKLPKAWVNIVPYRETGilaaK 228
Cdd:cd01982 144 QIEPKPFVQGRKGTVNIIGPSYGCFNSPSDLAEVKRLVTGIGAEVNHVYPFESHLAEIPKLKNAAVNVVMYREFG----R 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 229 WLKENFNIPYIStTPLGHENLAIWIKELEYCLkskGRVNLNFNNFIENKTTFNSQSFWFSRSidcQNLIGKSAVVFG--- 305
Cdd:cd01982 220 GLAEDLGRPYLY-APFGIEETTAFLRELGRLL---GLDPEAFIFREEEKRLTLLPVWWLWRG---PQFEWFPTFRFCata 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 306 DSTHVAAITKILKKDLGINILwagtycisdqnwFKHTLKEYTNNifvsenySVVEKLIKIASPDAIFGTQMER------- 378
Cdd:cd01982 293 TKSYAAGGLLELLLELGMQCL------------FSRDAGEKDND-------EPVRIEIRQKQPQFLFGRMNDKiylaetl 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1833819266 379 --HVGKKLGIPCGVISAPIhiqNYPIGyRPFFGYEGANQLIDMIYNTF 424
Cdd:cd01982 354 akHRFIPAFIPAPFPGRAL---RRPTG-TPFMGYWGAQEIVQELYNRL 397
|
|
| Nitrogenase_NifE_I |
cd01968 |
Nitrogenase_NifE_I: a subgroup of the NifE subunit of the NifEN complex: NifE forms an ... |
56-412 |
7.38e-11 |
|
Nitrogenase_NifE_I: a subgroup of the NifE subunit of the NifEN complex: NifE forms an alpha2beta2 tetramer with NifN. NifE and NifN are structurally homologous to nitrogenase MoFe protein alpha and beta subunits respectively. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of the MoFe protein. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to the NifEN complex where it is further processed to FeMoco. The NifEN bound precursor of FeMoco has been identified as a molybdenum-free, iron- and sulfur- containing analog of FeMoco. It has been suggested that this NifEN bound precursor also acts as a cofactor precursor in nitrogenase systems which require a cofactor other than FeMoco: i.e. iron-vanadium cofactor (FeVco) or iron only cofactor (FeFeco).
Pssm-ID: 238930 [Multi-domain] Cd Length: 410 Bit Score: 63.88 E-value: 7.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 56 TTNIIDRHVLTqGSANKIIRNIIRKDKEESPKLILITPTCTSSILQEDLDNFIKKSSLETNADVLLADINHY---RNNEY 132
Cdd:cd01968 58 STDLSEKDVIF-GGEKKLYKAILEIIERYHPKAVFVYSTCVVALIGDDIDAVCKTASEKFGIPVIPVHSPGFvgnKNLGN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 133 QAA-DITLKQIIHFYIKKYTNskisltkEPSVNIIGAYSLAfhnqHDILELIKVLTELNIKINLILPKGASIEELEKLPK 211
Cdd:cd01968 137 KLAcEALLDHVIGTEEPEPLT-------PYDINLIGEFNVA----GELWGVKPLLEKLGIRVLASITGDSRVDEIRRAHR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 212 AWVNIVPYRETGILAAKWLKENFNIPYISTTPLGHENLAIWIKELEYCLKSKGRVNLNfNNFI---ENKTTFNSQSFwfs 288
Cdd:cd01968 206 AKLNVVQCSKSMIYLARKMEEKYGIPYIEVSFYGIRDTSKSLRNIAELLGDEELIERT-EELIareEARLRPELAPY--- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 289 RSIdcqnLIGKSAVVFGDSTHVAAITKILkKDLGINILWAGTYCISDQNwfKHTLKEYT---NNIFVSENYSVVEKLIKI 365
Cdd:cd01968 282 RAR----LEGKKAALYTGGVKSWSLVSAL-QDLGMEVVATGTQKGTKED--YERIKELLgegTVIVDDANPRELKKLLKE 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1833819266 366 ASPDAIFGTQMERHVGKKLGIP-CGVISAPIHiqnypigyrPFFGYEG 412
Cdd:cd01968 355 KKADLLVAGGKERYLALKLGIPfCDINHERKH---------PYAGYEG 393
|
|
| Nitrogenase_NifN_2 |
cd03466 |
Nitrogenase_nifN_2: A subgroup of the NifN subunit of the NifEN complex: NifN forms an ... |
68-423 |
7.96e-11 |
|
Nitrogenase_nifN_2: A subgroup of the NifN subunit of the NifEN complex: NifN forms an alpha2beta2 tetramer with NifE. NifN and nifE are structurally homologous to nitrogenase MoFe protein beta and alpha subunits respectively. NifEN participates in the synthesis of the iron-molybdenum cofactor (FeMoco) of the MoFe protein. NifB-co (an iron and sulfur containing precursor of the FeMoco) from NifB is transferred to the NifEN complex where it is further processed to FeMoco. The nifEN bound precursor of FeMoco has been identified as a molybdenum-free, iron- and sulfur- containing analog of FeMoco. It has been suggested that this nifEN bound precursor also acts as a cofactor precursor in nitrogenase systems which require a cofactor other than FeMoco: i.e. iron-vanadium cofactor (FeVco) or iron only cofactor (FeFeco). This group also contains the Clostidium fused NifN-NifB protein.
Pssm-ID: 239549 [Multi-domain] Cd Length: 429 Bit Score: 63.95 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 68 GSAN--KIIRNIIRKDKeesPKLILITPTCTSSILQEDLDNFIKKSSLETNAD---VLLADINHYRNNEYQAADITLKQI 142
Cdd:cd03466 68 GEKNlkKGLKNVIEQYN---PEVIGIATTCLSETIGEDVPRIIREFREEVDDSepkIIPASTPGYGGTHVEGYDTAVRSI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 143 IHfYIKKYTnskislTKEPSVNII-GAYSLAfhnqhDILELIKVLTELNIKInLILP-------------------KGAS 202
Cdd:cd03466 145 VK-NIAVDP------DKIEKINVIaGMMSPA-----DIREIKEILREFGIEY-ILLPdtsetldgpfwgeyhrlpsGGTP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 203 IEELEKL--PKAWVNIVPYRETGILAAKWLKENFNIPYIS-TTPLGHENLAIWIKELEYClkskgrvnlnFNNFIENKTT 279
Cdd:cd03466 212 ISEIKGMggAKATIELGMFVDHGLSAGSYLEEEFGIPNYRlPLPIGLRATDEFMSLLSKL----------TGKPIPEKYT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 280 FNSqsfwfSRSIDC-----QNLIGKSAVVFGDSTHVAAITKILKkDLGI--NILWAGTYCISDQNWFKHTLKEYTNNIFV 352
Cdd:cd03466 282 RER-----GRLLDAmidahKYNFGRKAAIYGEPDFVVAITRFVL-ENGMvpVLIATGSESKKLKEKLEEDLKEYVEKCVI 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1833819266 353 SE--NYSVVEKLIKIASPDAIFGTQMERHVGKKLGIPCGVISAPIHIQnypIGYR--PFFGYEGANQLIDMIYNT 423
Cdd:cd03466 356 LDgaDFFDIESYAKELKIDVLIGNSYGRRIAEKLGIPLIRIGFPIHDR---LGGQriRSLGYEGSIELVDRITNT 427
|
|
| Nitrogenase_VFe_alpha |
cd01977 |
Nitrogenase_VFe_alpha -like: Nitrogenase VFe protein, alpha subunit like. This group contains ... |
8-422 |
1.43e-10 |
|
Nitrogenase_VFe_alpha -like: Nitrogenase VFe protein, alpha subunit like. This group contains proteins similar to the alpha subunits of, the VFe protein of the vanadium-dependent (V-) nitrogenase and the FeFe protein of the iron only (Fe-) nitrogenase Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen (N2) to ammonia. In addition to V- and Fe- nitrogenases there is a molybdenum (Mo)-dependent nitrogenase which is the most widespread and best characterized of these systems. These systems consist of component 1 (VFe protein, FeFe protein or, MoFe protein respectively) and, component 2 (Fe protein). MoFe is an alpha2beta2 tetramer, V-and Fe- nitrogenases are alpha2beta2delta2 hexamers. The alpha and beta subunits of VFe and FeFe are similar to the alpha and beta subunits of MoFe. For MoFe each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein which has a practically identical structure in all three systems, it contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo-nitrogenase in that it produces free hydrazine, as a minor product during dinitrogen reduction and, ethane as a minor product during acetylene reduction.
Pssm-ID: 238936 [Multi-domain] Cd Length: 415 Bit Score: 63.23 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 8 YAGPAHIgtlrIASSFQNVLAIMHAPLGDDYF-NVMRSMLERQKNLP---KVTTNIIDRHVLTqGSANKIIRNIIRKDKE 83
Cdd:cd01977 11 YCGAKLV----IGGVIKDVIHVIHGPVGCTYDtWHTKRYPSDNDNFQlkyIWSTDMKESHVVF-GGEKKLKKNIIEAFKE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 84 -ESPKLILITPTCTSSILQEDLDNFIKKSSLEtnadvlLADINHYRNNEYQAADITLKQIIHFYIKKYTNSKISlTKEP- 161
Cdd:cd01977 86 fPDIKRMTVYTTCTTALIGDDIKAVAKEVMEE------LPDVDIFVCNAPGFAGPSQSKGHHVLNIAWINQKVG-TVEPe 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 162 -----SVNIIGAYSLafhnQHDILELIKVLTELNIKINLILPKGASIEELEKLPKAWVNIVPYRETGILAAKWLKENFNI 236
Cdd:cd01977 159 itsdyTINYIGDYNI----QGDTEVLQKYFERMGIQVLSTFTGNGTYDDLRWMHRAKLNVVNCARSAGYIANELKKRYGI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 237 PYISTTPLGhenlaiwikeLEYCLKSKGRVNLNFNNFIENKTTFNSQSFWFSRSIDC--QNLIGKSAVVFGDSTHVAAIT 314
Cdd:cd01977 235 PRLDVDGFG----------FEYCAESLRKIGAFFGIEDRAEAVIAEEMAKWKPELDWykERLKGKKVCIWTGGPKLWHWT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 315 KILKKDLGINILWAGTYCISDQNWFKHTLKEYTNNIFVSE-NYSVVEKLIKIASPDAIFGTQMERHVGKKLGIPCgvisa 393
Cdd:cd01977 305 KVIEDELGMQVVAMSSKFGHQEDFEKVIARGGEGTIYIDDpNELEFFEILEMLKPDIILTGPRVGELVKKLHVPY----- 379
|
410 420
....*....|....*....|....*....
gi 1833819266 394 pIHIQNYPIGyrPFFGYEGANQLIDMIYN 422
Cdd:cd01977 380 -VNIHAYHNG--PYMGFEGFVNLARDMYN 405
|
|
| PCP_red |
pfam08369 |
Proto-chlorophyllide reductase 57 kD subunit; This domain is found in bacteria and plant ... |
457-501 |
2.72e-08 |
|
Proto-chlorophyllide reductase 57 kD subunit; This domain is found in bacteria and plant chloroplast proteins. It often appears at the C-terminal of Nitrogenase component 1 type Oxidoreductases (pfam00148) and sometimes independently in bacterial proteins such as the Proto-chlorophyllide reductase 57 kD subunit of the Cyanobacterium Synechocystis.
Pssm-ID: 462449 [Multi-domain] Cd Length: 45 Bit Score: 49.78 E-value: 2.72e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1833819266 457 WTKEAENIFAQIPKIFQKKIKHKIDTYAASLNKTIVTPEILYKAK 501
Cdd:pfam08369 1 WTDEAEARLKKIPFFVRKKARRNAEKYARERGLEEVTVEVVEEAK 45
|
|
| nifE |
TIGR01283 |
nitrogenase molybdenum-iron cofactor biosynthesis protein NifE; This protein is part of the ... |
68-239 |
4.68e-08 |
|
nitrogenase molybdenum-iron cofactor biosynthesis protein NifE; This protein is part of the NifEN complex involved in biosynthesis of the molybdenum-iron cofactor used by the homologous NifDK complex of nitrogenase. In a few species, the protein is found as a NifEN fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Central intermediary metabolism, Nitrogen fixation]
Pssm-ID: 188126 [Multi-domain] Cd Length: 453 Bit Score: 55.44 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 68 GSANKIIRNIIRKDKEESPKLILITPTCTSSILQEDLDNFIKKSSLETNADVLLAD---INHYRNNEYQAA-DITLKQII 143
Cdd:TIGR01283 101 GGEKKLFHAIREIVERYHPPAVFVYSTCVPALIGDDLEAVCKAAAEKTGIPVIPVDsegFYGTKNLGNKLAcDALLKHVI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 144 HfyiKKYTNSKISLTKEPSVNIIGAYSLAfhnqHDILELIKVLTELNIKINLILPKGASIEELEKLPKAWVNIVPYRETG 223
Cdd:TIGR01283 181 G---TREPEPLPVGITVHDINLIGEFNVA----GEFWHVLPLLEKLGIRVLATITGDSRYAEVQTAHRAKLNMVQCSKAM 253
|
170
....*....|....*.
gi 1833819266 224 ILAAKWLKENFNIPYI 239
Cdd:TIGR01283 254 INLARKMEEKYGIPYF 269
|
|
| Nitrogenase_MoFe_beta |
cd01974 |
Nitrogenase_MoFe_beta: Nitrogenase MoFe protein, beta subunit. The nitrogenase enzyme ... |
86-424 |
2.93e-05 |
|
Nitrogenase_MoFe_beta: Nitrogenase MoFe protein, beta subunit. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen to ammonia. The Molybdenum (Mo-) nitrogenase is the most widespread and best characterized of these systems. Mo-nitrogenase consists of the MoFe protein (component 1) and the Fe protein (component 2). MoFe is an alpha2beta2 tetramer. This group contains the beta subunit of the MoFe protein. Each alphabeta pair of MoFe contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction.
Pssm-ID: 238934 [Multi-domain] Cd Length: 435 Bit Score: 46.50 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 86 PKLILITPTCTSSILQEDLDNFIKKS----SLETNADVLLADINHYRNNEYQAADITLKQIihfyIKKYTNSKISLTKEP 161
Cdd:cd01974 86 PDMIAVSTTCMAEVIGDDLNAFIKNAknkgSIPADFPVPFANTPSFVGSHITGYDNMVKGI----LTHLTEGSGGAGKNG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 162 SVNIIGayslAFHNQHDILELIKVLTEL-NIKINLI-----------------LPKGASIEELEKLPKAWVNIVPYRETG 223
Cdd:cd01974 162 KLNIIP----GFDTYAGNMREIKRLLELmGVDYTILpdtsdvldtpadgeyrmYPGGTTLEELKDAGNAKATLALQEYAT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 224 ILAAKWLKENFNIPYIS-TTPLGHENLAIWIKELeyclkSKgrvnlnfnnfIENKTTFNSQSFWFSRSIDC-----QNLI 297
Cdd:cd01974 238 EKTAKFLEKKCKVPVETlNMPIGVAATDEFLMAL-----SE----------LTGKPIPEELEEERGRLVDAmtdshQYLH 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 298 GKSAVVFGDSTHVAAITKILkKDLG---INILwagtyCISDQNWFKHTLKEYTNNIFVSENYSV--------VEKLIKIA 366
Cdd:cd01974 303 GKKFALYGDPDFLIGLTSFL-LELGmepVHVL-----TGNGGKRFEKEMQALLDASPYGAGAKVypgkdlwhLRSLLFTE 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1833819266 367 SPDAIFGTQMERHVGKKLGIPCGVISAPI----HIQNYPIgyrpfFGYEGANQLIDMIYNTF 424
Cdd:cd01974 377 PVDLLIGNTYGKYIARDTDIPLVRFGFPIfdrhHHHRFPI-----VGYEGALRLLTTILNTL 433
|
|
| Nitrogenase_VFe_beta_like |
cd01973 |
Nitrogenase_VFe_beta -like: Nitrogenase VFe protein, beta subunit like. This group contains ... |
87-256 |
4.12e-05 |
|
Nitrogenase_VFe_beta -like: Nitrogenase VFe protein, beta subunit like. This group contains proteins similar to the beta subunits of the VFe protein of the vanadium-dependent (V-) nitrogenase. Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen (N2) to ammonia. In addition to V-nitrogenase there is a molybdenum (Mo)-dependent nitrogenase and an iron only (Fe-) nitrogenase. The Mo-nitrogenase is the most widespread and best characterized of these systems. These systems consist of component 1 (VFe protein, FeFe protein or, MoFe protein respectively) and, component 2 (Fe protein). MoFe is an alpha2beta2 tetramer, V-and Fe- nitrogenases are alpha2beta2delta2 hexamers. The alpha and beta subunits of VFe and FeFe are similar to the alpha and beta subunits of MoFe. For MoFe each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein which has a practically identical structure in all three systems, it contains a single [4Fe-4S] cluster. Electrons are transferred from the [4Fe-4S] cluster of the Fe protein to the P-cluster of the MoFe and in turn to FeMoCo, the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo-nitrogenase in that it produces free hydrazine, as a minor product during dinitrogen reduction and, ethane as a minor product during acetylene reduction.
Pssm-ID: 238933 [Multi-domain] Cd Length: 454 Bit Score: 45.94 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 87 KLILITPTCTSSILQEDLDNFIKK--SSLET---NADVLLADIN--HYRNNEYQAADITLKQIIHFYIKKytnskisltK 159
Cdd:cd01973 89 RVIPIITTCSTEIIGDDIEGVIRKlnEALKEefpDREVHLIPVHtpSFKGSMVTGYDEAVRSVVKTIAKK---------G 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819266 160 EPS--VNIIGAYSlafhNQHDILELIKVLTELNIKINL----------ILPKGAS-------IEELEKLPKAWVNIVPYR 220
Cdd:cd01973 160 APSgkLNVFTGWV----NPGDVVELKHYLSEMDVEANIlmdtedfdspMLPDKSAvthgnttIEDIADSANAIATIALAR 235
|
170 180 190
....*....|....*....|....*....|....*..
gi 1833819266 221 ETGILAAKWLKENFNIP-YISTTPLGHENLAIWIKEL 256
Cdd:cd01973 236 YEGGKAAEFLQKKFDVPaILGPTPIGIKNTDAFLQNI 272
|
|
| |
