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Conserved domains on  [gi|1002248084|ref|XP_015628216|]
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tryptophan synthase alpha chain [Oryza sativa Japonica Group]

Protein Classification

tryptophan synthase subunit alpha( domain architecture ID 10791415)

Tryptophan synthase (TRPS) alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P).

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02591 PLN02591
tryptophan synthase
 30-279 7.68e-171

tryptophan synthase


:

Pssm-ID: 178201  Cd Length: 250  Bit Score: 472.23  E-value: 7.68e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  30 KTAFIPFITASDPDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRALKKGATFDSVIAMLKGVIPELSCP 109
Cdd:PLN02591    1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 110 IVIFTYYNPILKRGVSNFMAIIKQAGVHGLVVPDLPLEETALLRNEAVMHGIELVLLTTPTTPTERMKEIAKASEGFIYL 189
Cdd:PLN02591   81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 190 VSSVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAIVRQLGEAASPEEGLKRVEE 269
Cdd:PLN02591  161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240

                         250
                  ....*....|
gi 1002248084 270 YAKNMKAAMP 279
Cdd:PLN02591  241 LAKSLKAALP 250
 
Name Accession Description Interval E-value
PLN02591 PLN02591
tryptophan synthase
 30-279 7.68e-171

tryptophan synthase


Pssm-ID: 178201  Cd Length: 250  Bit Score: 472.23  E-value: 7.68e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  30 KTAFIPFITASDPDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRALKKGATFDSVIAMLKGVIPELSCP 109
Cdd:PLN02591    1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 110 IVIFTYYNPILKRGVSNFMAIIKQAGVHGLVVPDLPLEETALLRNEAVMHGIELVLLTTPTTPTERMKEIAKASEGFIYL 189
Cdd:PLN02591   81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 190 VSSVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAIVRQLGEAASPEEGLKRVEE 269
Cdd:PLN02591  161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240

                         250
                  ....*....|
gi 1002248084 270 YAKNMKAAMP 279
Cdd:PLN02591  241 LAKSLKAALP 250
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 18-278 1.42e-114

Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase alpha chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439929  Cd Length: 262  Bit Score: 330.10  E-value: 1.42e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  18 VAETFSRLREQGKTAFIPFITASDPDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRALKKGATFDSVIA 97
Cdd:COG0159     3 IDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  98 MLKGVIPELSCPIVIFTYYNPILKRGVSNFMAIIKQAGVHGLVVPDLPLEETALLRNEAVMHGIELVLLTTPTTPTERMK 177
Cdd:COG0159    83 LVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 178 EIAKASEGFIYLVSSVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWgADGVIIGSAIVRQLgEA 257
Cdd:COG0159   163 KIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLI-EE 240

                         250       260
                  ....*....|....*....|.
gi 1002248084 258 ASPEEGLKRVEEYAKNMKAAM 278
Cdd:COG0159   241 GGDDEALEALAAFVRELKAAL 261
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
22-277 2.59e-113

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 326.96  E-value: 2.59e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  22 FSRLREQGKTAFIPFITASDPDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRALKKGATFDSVIAMLKG 101
Cdd:pfam00290   1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 102 V-IPELSCPIVIFTYYNPILKRGVSNFMAIIKQAGVHGLVVPDLPLEETALLRNEAVMHGIELVLLTTPTTPTERMKEIA 180
Cdd:pfam00290  81 VrSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 181 KASEGFIYLVSSVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAgWGADGVIIGSAIVRQLGEAA-S 259
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAA-AGADGVIVGSALVRIIEEAAdG 239

                         250
                  ....*....|....*...
gi 1002248084 260 PEEGLKRVEEYAKNMKAA 277
Cdd:pfam00290 240 PEQGLARLEELAGEMKAA 257
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 32-275 1.80e-108

Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 alpha and 2 beta subunits) that catalyzes the last two steps of L-tryptophan biosynthesis. Alpha and beta subunit catalyze two distinct reactions which are both strongly stimulated by the formation of the complex. The alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P). Indole is then channeled to the active site of the beta subunit, a PLP-dependent enzyme that catalyzes a replacement reaction to convert L-serine into L-tryptophan.


Pssm-ID: 240075  Cd Length: 242  Bit Score: 314.03  E-value: 1.80e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  32 AFIPFITASDPDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRALKKGATFDSVIAMLKGVIPELSCPIV 111
Cdd:cd04724     1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 112 IFTYYNPILKRGVSNFMAIIKQAGVHGLVVPDLPLEETALLRNEAVMHGIELVLLTTPTTPTERMKEIAKASEGFIYLVS 191
Cdd:cd04724    81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 192 SVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWgADGVIIGSAIVRQLGEAAsPEEGLKRVEEYA 271
Cdd:cd04724   161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEGG-EEEALEALKELA 238


                  ....
gi 1002248084 272 KNMK 275
Cdd:cd04724   239 ESLK 242
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 22-275 6.08e-102

tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. The alpha chain is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria and plants each domain is found on a separate subunit (alpha and beta chains), while in fungi the two domains are fused together on a single multifunctional protein. The signature pattern for trpA contains three conserved acidic residues. [LIVM]-E-[LIVM]-G-x(2)-[FYC]-[ST]-[DE]-[PA]-[LIVMY]-[AGLI]-[DE]-G and this is located between residues 43-58 of the model. The Sulfolobus solfataricus trpA is known to be quite divergent from other known trpA sequences. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 161792  Cd Length: 256  Bit Score: 297.72  E-value: 6.08e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  22 FSRLREQGKTAFIPFITASDPDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRALKKGATFDSVIAMLKG 101
Cdd:TIGR00262   1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 102 VIPEL-SCPIVIFTYYNPILKRGVSNFMAIIKQAGVHGLVVPDLPLEETALLRNEAVMHGIELVLLTTPTTPTERMKEIA 180
Cdd:TIGR00262  81 VRQKHpNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 181 KASEGFIYLVSSVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAIVRQLGE-AAS 259
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIEEnLNT 240

                         250
                  ....*....|....*.
gi 1002248084 260 PEEGLKRVEEYAKNMK 275
Cdd:TIGR00262 241 PEKMLQALEEFVQNLK 256
 
Name Accession Description Interval E-value
PLN02591 PLN02591
tryptophan synthase
 30-279 7.68e-171

tryptophan synthase


Pssm-ID: 178201  Cd Length: 250  Bit Score: 472.23  E-value: 7.68e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  30 KTAFIPFITASDPDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRALKKGATFDSVIAMLKGVIPELSCP 109
Cdd:PLN02591    1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 110 IVIFTYYNPILKRGVSNFMAIIKQAGVHGLVVPDLPLEETALLRNEAVMHGIELVLLTTPTTPTERMKEIAKASEGFIYL 189
Cdd:PLN02591   81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 190 VSSVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAIVRQLGEAASPEEGLKRVEE 269
Cdd:PLN02591  161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240

                         250
                  ....*....|
gi 1002248084 270 YAKNMKAAMP 279
Cdd:PLN02591  241 LAKSLKAALP 250
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 20-278 2.87e-116

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237285  Cd Length: 258  Bit Score: 334.38  E-value: 2.87e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  20 ETFSRLREQGKTAFIPFITASDPDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRALKKGATFDSVIAML 99
Cdd:PRK13111    1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 100 KGV-IPELSCPIVIFTYYNPILKRGVSNFMAIIKQAGVHGLVVPDLPLEETALLRNEAVMHGIELVLLTTPTTPTERMKE 178
Cdd:PRK13111   81 REIrEKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 179 IAKASEGFIYLVSSVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAGwGADGVIIGSAIVRQLGEAa 258
Cdd:PRK13111  161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAA-VADGVIVGSALVKIIEEN- 238

                         250       260
                  ....*....|....*....|
gi 1002248084 259 spEEGLKRVEEYAKNMKAAM 278
Cdd:PRK13111  239 --PEALEALAAFVKELKAAL 256
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 18-278 1.42e-114

Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase alpha chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439929  Cd Length: 262  Bit Score: 330.10  E-value: 1.42e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  18 VAETFSRLREQGKTAFIPFITASDPDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRALKKGATFDSVIA 97
Cdd:COG0159     3 IDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  98 MLKGVIPELSCPIVIFTYYNPILKRGVSNFMAIIKQAGVHGLVVPDLPLEETALLRNEAVMHGIELVLLTTPTTPTERMK 177
Cdd:COG0159    83 LVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 178 EIAKASEGFIYLVSSVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWgADGVIIGSAIVRQLgEA 257
Cdd:COG0159   163 KIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLI-EE 240

                         250       260
                  ....*....|....*....|.
gi 1002248084 258 ASPEEGLKRVEEYAKNMKAAM 278
Cdd:COG0159   241 GGDDEALEALAAFVRELKAAL 261
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
22-277 2.59e-113

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 326.96  E-value: 2.59e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  22 FSRLREQGKTAFIPFITASDPDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRALKKGATFDSVIAMLKG 101
Cdd:pfam00290   1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 102 V-IPELSCPIVIFTYYNPILKRGVSNFMAIIKQAGVHGLVVPDLPLEETALLRNEAVMHGIELVLLTTPTTPTERMKEIA 180
Cdd:pfam00290  81 VrSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 181 KASEGFIYLVSSVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAgWGADGVIIGSAIVRQLGEAA-S 259
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAA-AGADGVIVGSALVRIIEEAAdG 239

                         250
                  ....*....|....*...
gi 1002248084 260 PEEGLKRVEEYAKNMKAA 277
Cdd:pfam00290 240 PEQGLARLEELAGEMKAA 257
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 32-275 1.80e-108

Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 alpha and 2 beta subunits) that catalyzes the last two steps of L-tryptophan biosynthesis. Alpha and beta subunit catalyze two distinct reactions which are both strongly stimulated by the formation of the complex. The alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P). Indole is then channeled to the active site of the beta subunit, a PLP-dependent enzyme that catalyzes a replacement reaction to convert L-serine into L-tryptophan.


Pssm-ID: 240075  Cd Length: 242  Bit Score: 314.03  E-value: 1.80e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  32 AFIPFITASDPDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRALKKGATFDSVIAMLKGVIPELSCPIV 111
Cdd:cd04724     1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 112 IFTYYNPILKRGVSNFMAIIKQAGVHGLVVPDLPLEETALLRNEAVMHGIELVLLTTPTTPTERMKEIAKASEGFIYLVS 191
Cdd:cd04724    81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 192 SVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWgADGVIIGSAIVRQLGEAAsPEEGLKRVEEYA 271
Cdd:cd04724   161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEGG-EEEALEALKELA 238


                  ....
gi 1002248084 272 KNMK 275
Cdd:cd04724   239 ESLK 242
trpA CHL00200
tryptophan synthase alpha subunit; Provisional
 15-277 1.88e-103

tryptophan synthase alpha subunit; Provisional


Pssm-ID: 214394  Cd Length: 263  Bit Score: 302.07  E-value: 1.88e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  15 KRGVAETFSRLREQgkTAFIPFITASDPDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRALKKGATFDS 94
Cdd:CHL00200    1 MNTISNVFEKLDKQ--CALIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  95 VIAMLKGVIPELSCPIVIFTYYNPILKRGVSNFMAIIKQAGVHGLVVPDLPLEETALLRNEAVMHGIELVLLTTPTTPTE 174
Cdd:CHL00200   79 ILSILSEVNGEIKAPIVIFTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAPTSSKS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 175 RMKEIAKASEGFIYLVSSVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAIVRQL 254
Cdd:CHL00200  159 RIQKIARAAPGCIYLVSTTGVTGLKTELDKKLKKLIETIKKMTNKPIILGFGISTSEQIKQIKGWNINGIVIGSACVQIL 238

                         250       260
                  ....*....|....*....|...
gi 1002248084 255 gEAASPEEGLKRVEEYAKNMKAA 277
Cdd:CHL00200  239 -LGSSPEKGLDQLSEFCKVAKKS 260
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 22-275 6.08e-102

tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. The alpha chain is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria and plants each domain is found on a separate subunit (alpha and beta chains), while in fungi the two domains are fused together on a single multifunctional protein. The signature pattern for trpA contains three conserved acidic residues. [LIVM]-E-[LIVM]-G-x(2)-[FYC]-[ST]-[DE]-[PA]-[LIVMY]-[AGLI]-[DE]-G and this is located between residues 43-58 of the model. The Sulfolobus solfataricus trpA is known to be quite divergent from other known trpA sequences. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 161792  Cd Length: 256  Bit Score: 297.72  E-value: 6.08e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  22 FSRLREQGKTAFIPFITASDPDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRALKKGATFDSVIAMLKG 101
Cdd:TIGR00262   1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 102 VIPEL-SCPIVIFTYYNPILKRGVSNFMAIIKQAGVHGLVVPDLPLEETALLRNEAVMHGIELVLLTTPTTPTERMKEIA 180
Cdd:TIGR00262  81 VRQKHpNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 181 KASEGFIYLVSSVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAIVRQLGE-AAS 259
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIEEnLNT 240

                         250
                  ....*....|....*.
gi 1002248084 260 PEEGLKRVEEYAKNMK 275
Cdd:TIGR00262 241 PEKMLQALEEFVQNLK 256
trpA PRK13125
tryptophan synthase subunit alpha; Provisional
 30-269 1.22e-20

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237286  Cd Length: 244  Bit Score: 88.17  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  30 KTAFIPFITASDPDLATTSKALKILDSCgSDVIELGVPYSDPLADGPVIqaaatRALKKGATFDSVIAMLKGVIPELSCP 109
Cdd:PRK13125    3 RPGLVVYLTAGYPNVESFKEFIIGLVEL-VDILELGIPPKYPKYDGPVI-----RKSHRKVKGLDIWPLLEEVRKDVSVP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 110 IVIFTYYNPILKRgVSNFMAIIKQAGVHGLVVPDLPL---EETALLRNEAVMHGIELVLLTTPTTPTERMKEIAKASEGF 186
Cdd:PRK13125   77 IILMTYLEDYVDS-LDNFLNMARDVGADGVLFPDLLIdypDDLEKYVEIIKNKGLKPVFFTSPKFPDLLIHRLSKLSPLF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 187 IYLvssvGVTGArSNVNLRVeYLLQEIKK----VTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAIVRQLgEAASPEE 262
Cdd:PRK13125  156 IYY----GLRPA-TGVPLPV-SVERNIKRvrnlVGNKYLVVGFGLDSPEDARDALSAGADGVVVGTAFIEEL-EKNGVES 228


                  ....*..
gi 1002248084 263 GLKRVEE 269
Cdd:PRK13125  229 ALNLLKK 235
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 36-248 3.88e-06

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 46.43  E-value: 3.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084  36 FITASD--PDLATTSKALKILDSCGSDVIELGVPYSDPLADGPVIQAAATRalkkgatfdsviamlkgVIPELSCPIVIF 113
Cdd:cd04722     1 VILALLagGPSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKE-----------------VAAETDLPLGVQ 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 114 TYYNPILKRgVSNFMAIIKQAGVHGLVVPDLPL---EETALLRNEAVMHGIELVLLTTPTTPTERMKEIAKASEGFIYLV 190
Cdd:cd04722    64 LAINDAAAA-VDIAAAAARAAGADGVEIHGAVGylaREDLELIRELREAVPDVKVVVKLSPTGELAAAAAEEAGVDEVGL 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002248084 191 SSVGVTGARSNVNLRVEYLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGS 248
Cdd:cd04722   143 GNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 209-252 4.47e-05

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 43.72  E-value: 4.47e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002248084 209 LLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAIVR 252
Cdd:cd04729   168 LLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSAITR 211
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 178-253 7.36e-05

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 42.85  E-value: 7.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 178 EIAKA--SEGFIYLVSsVGVTGARSN--VNLRVeylLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAIVRQ 253
Cdd:pfam00977  33 ELAKRyeEEGADELHF-VDLDAAKEGrpVNLDV---VEEIAEEVFIPVQVGGGIRSLEDVERLLSAGADRVIIGTAAVKN 108
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 209-250 1.07e-04

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 42.72  E-value: 1.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1002248084 209 LLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAI 250
Cdd:COG0106   180 LYRELAAATGIPVIASGGVSSLDDLRALKELGVEGAIVGKAL 221
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 209-250 1.14e-04

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240074 [Multi-domain]  Cd Length: 233  Bit Score: 42.64  E-value: 1.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1002248084 209 LLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAI 250
Cdd:cd04723   180 LLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASAL 221
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
 226-267 1.48e-04

Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.


Pssm-ID: 238203  Cd Length: 217  Bit Score: 42.07  E-value: 1.48e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1002248084 226 GISTPEHVKQIAGWGADGVIIGSAIVRqlgeAASPEEGLKRV 267
Cdd:cd00331   180 GISTPEDVKRLAEAGADAVLIGESLMR----APDPGAALREL 217
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 189-250 1.79e-04

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 41.70  E-value: 1.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002248084 189 LVSSVGVTGARSNVNLRveyLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAI 250
Cdd:pfam00977 164 LLTDIDRDGTLSGPDLE---LTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSAL 222
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
209-252 2.15e-04

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 41.67  E-value: 2.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002248084 209 LLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAIVR 252
Cdd:PRK01130  164 LLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITR 207
trpC PRK00278
indole-3-glycerol phosphate synthase TrpC;
226-266 2.36e-04

indole-3-glycerol phosphate synthase TrpC;


Pssm-ID: 234710  Cd Length: 260  Bit Score: 41.68  E-value: 2.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1002248084 226 GISTPEHVKQIAGWGADGVIIGSAIVRQlgeaASPEEGLKR 266
Cdd:PRK00278  219 GIFTPEDLKRLAKAGADAVLVGESLMRA----DDPGAALRE 255
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 209-250 3.75e-04

HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.


Pssm-ID: 240083  Cd Length: 234  Bit Score: 40.93  E-value: 3.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1002248084 209 LLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAI 250
Cdd:cd04732   181 LYKELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKAL 222
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 197-253 4.68e-04

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 40.41  E-value: 4.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002248084 197 GARS--NVNLRVeylLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAIVRQ 253
Cdd:COG0106    53 GAFAgkPVNLEL---IEEIAKATGLPVQVGGGIRSLEDIERLLDAGASRVILGTAAVKD 108
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 209-277 7.12e-04

Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440121 [Multi-domain]  Cd Length: 206  Bit Score: 39.78  E-value: 7.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 209 LLQEIKKVTDKP-VAVGfGIsTPEHVKQIAGWGADGVIIGSAIVRqlgeAASPEEglkRVEEYAKNMKAA 277
Cdd:COG0352   146 GLAWWAELVEIPvVAIG-GI-TPENAAEVLAAGADGVAVISAIWG----APDPAA---AARELRAALEAA 206
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 196-253 8.44e-04

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated


Pssm-ID: 179108  Cd Length: 233  Bit Score: 39.66  E-value: 8.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 196 TGARS--NVNLRveyLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAIVRQ 253
Cdd:PRK00748   53 DGAKAgkPVNLE---LIEAIVKAVDIPVQVGGGIRSLETVEALLDAGVSRVIIGTAAVKN 109
GGGP-family TIGR01768
geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of ...
 209-250 2.97e-03

geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of sequences including geranylgeranylglyceryl phosphate synthase which catalyzes the first committed step in the synthesis of ether-linked membrane lipids in archaea. The clade of bacterial sequences may have the same function or a closely related function. This model supercedes TIGR00265, which has been retired.


Pssm-ID: 273794  Cd Length: 223  Bit Score: 38.23  E-value: 2.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1002248084 209 LLQEIKKVTDK-PVAVGFGISTPEHVKQIAGWGADGVIIGSAI 250
Cdd:TIGR01768 169 LVAEVKKVLDKaRLFVGGGIRSVEKAREMAEAGADTVVTGNVI 211
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 193-270 2.97e-03

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272850 [Multi-domain]  Cd Length: 230  Bit Score: 38.33  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248084 193 VGVTGARSN--VNLRVeylLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAIVRqlgeaaSPEEGLKRVEEY 270
Cdd:TIGR00007  48 VDLDGAKEGgpVNLPV---IKKIVRETGVPVQVGGGIRSLEDVEKLLDLGVDRVIIGTAAVE------NPDLVKELLKEY 118
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 209-266 4.12e-03

Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.


Pssm-ID: 238317 [Multi-domain]  Cd Length: 196  Bit Score: 37.50  E-value: 4.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002248084 209 LLQEIKKVTDKP-VAVGfGIsTPEHVKQIAGWGADGVIIGSAIVRqlgeAASPEEGLKR 266
Cdd:cd00564   141 LLREIAELVEIPvVAIG-GI-TPENAAEVLAAGADGVAVISAITG----ADDPAAAARE 193
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 174-250 4.74e-03

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272850 [Multi-domain]  Cd Length: 230  Bit Score: 37.56  E-value: 4.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002248084 174 ERMKEIAkaSEGFIYlvSSVGVTGARSNVNLRveyLLQEIKKVTDKPVAVGFGISTPEHVKQIAGWGADGVIIGSAI 250
Cdd:TIGR00007 152 KRLEELG--LEGIIY--TDISRDGTLSGPNFE---LTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKAL 221
PcrB_like cd02812
PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been ...
 209-250 7.50e-03

PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been characterized as a (S)-3-O-geranylgeranylglyceryl phosphate synthase (AfGGGPS). AfGGGPS catalyzes the formation of an ether linkage between sn-glycerol-1-phosphate (G1P) and geranylgeranyl diphosphate (GGPP), the committed step in archaeal lipid biosynthesis. Therefore, it has been proposed that PcrB-like proteins are either prenyltransferases or are involved in lipoteichoic acid biosynthesis although the exact function is still unknown.


Pssm-ID: 239206  Cd Length: 219  Bit Score: 36.83  E-value: 7.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1002248084 209 LLQEIKKVTDK-PVAVGFGISTPEHVKQIAGWGADGVIIGSAI 250
Cdd:cd02812   165 VVRAVKKVLGDtPLIVGGGIRSGEQAKEMAEAGADTIVVGNIV 207
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 188-250 7.83e-03

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 36.86  E-value: 7.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002248084 188 YLVSSVGVTGARSNVNLRveyLLQEIKKVTDKPVAVGFGISTPEHVKQIAGW---GADGVIIGSAI 250
Cdd:PRK14024  163 YVVTDVTKDGTLTGPNLE---LLREVCARTDAPVVASGGVSSLDDLRALAELvplGVEGAIVGKAL 225
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 209-262 9.61e-03

3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.


Pssm-ID: 240077 [Multi-domain]  Cd Length: 202  Bit Score: 36.40  E-value: 9.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002248084 209 LLQEIKKVTDKPVAVGFGIsTPEHVKQIAGWGADGVIIGSAIVRqlgeAASPEE 262
Cdd:cd04726   149 DLKKVKKLLGVKVAVAGGI-TPDTLPEFKKAGADIVIVGRAITG----AADPAE 197
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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