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Conserved domains on  [gi|15235430|ref|NP_192170|]
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Aldolase-type TIM barrel family protein [Arabidopsis thaliana]

Protein Classification

tryptophan synthase subunit alpha( domain architecture ID 10791415)

tryptophan synthase (TRPS) alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate

CATH:  3.20.20.70
EC:  4.2.1.20
Gene Ontology:  GO:0004834|GO:0006568
PubMed:  2679363
SCOP:  4003071

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02591 PLN02591
tryptophan synthase
 25-273 8.50e-177

tryptophan synthase


:

Pssm-ID: 178201  Cd Length: 250  Bit Score: 486.87  E-value: 8.50e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430   25 KVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIISMLKEVIPQLSCP 104
Cdd:PLN02591   1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  105 IALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMNAIVEASEGFIYL 184
Cdd:PLN02591  81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  185 VSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVKILGESESPEQGLKELEF 264
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240


                 ....*....
gi 15235430  265 FTKSLKSAL 273
Cdd:PLN02591 241 LAKSLKAAL 249
 
Name Accession Description Interval E-value
PLN02591 PLN02591
tryptophan synthase
 25-273 8.50e-177

tryptophan synthase


Pssm-ID: 178201  Cd Length: 250  Bit Score: 486.87  E-value: 8.50e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430   25 KVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIISMLKEVIPQLSCP 104
Cdd:PLN02591   1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  105 IALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMNAIVEASEGFIYL 184
Cdd:PLN02591  81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  185 VSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVKILGESESPEQGLKELEF 264
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240


                 ....*....
gi 15235430  265 FTKSLKSAL 273
Cdd:PLN02591 241 LAKSLKAAL 249
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 13-273 6.16e-125

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: 356.30  E-value: 6.16e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  13 LSETFARLKSQGKVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIIS 92
Cdd:COG0159   3 IDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  93 MLKEVIPQLSCPIALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMN 172
Cdd:COG0159  83 LVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIK 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430 173 AIVEASEGFIYLVSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWgADGVIVGSAMVKILGES 252
Cdd:COG0159 163 KIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLIEEG 241

                       250       260
                ....*....|....*....|.
gi 15235430 253 EsPEQGLKELEFFTKSLKSAL 273
Cdd:COG0159 242 G-DDEALEALAAFVRELKAAL 261
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 27-270 1.88e-118

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: 339.07  E-value: 1.88e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  27 ALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIISMLKEVIPQLSCPIA 106
Cdd:cd04724   1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430 107 LFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMNAIVEASEGFIYLVS 186
Cdd:cd04724  81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430 187 SVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWgADGVIVGSAMVKILGESeSPEQGLKELEFFT 266
Cdd:cd04724 161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEG-GEEEALEALKELA 238


                ....
gi 15235430 267 KSLK 270
Cdd:cd04724 239 ESLK 242
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
17-273 3.14e-112

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 323.88  E-value: 3.14e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430    17 FARLKSQGKVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIISMLKE 96
Cdd:pfam00290   1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430    97 V-IPQLSCPIALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMNAIV 175
Cdd:pfam00290  81 VrSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430   176 EASEGFIYLVSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAeWGADGVIVGSAMVKILGES-ES 254
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAA-AGADGVIVGSALVRIIEEAaDG 239

                         250
                  ....*....|....*....
gi 15235430   255 PEQGLKELEFFTKSLKSAL 273
Cdd:pfam00290 240 PEQGLARLEELAGEMKAAA 258
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 17-270 1.40e-106

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: 309.66  E-value: 1.40e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430    17 FARLKSQGKVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIISMLKE 96
Cdd:TIGR00262   1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430    97 VIPQL-SCPIALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMNAIV 175
Cdd:TIGR00262  81 VRQKHpNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430   176 EASEGFIYLVSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVKILGES-ES 254
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIEENlNT 240

                         250
                  ....*....|....*.
gi 15235430   255 PEQGLKELEFFTKSLK 270
Cdd:TIGR00262 241 PEKMLQALEEFVQNLK 256
 
Name Accession Description Interval E-value
PLN02591 PLN02591
tryptophan synthase
 25-273 8.50e-177

tryptophan synthase


Pssm-ID: 178201  Cd Length: 250  Bit Score: 486.87  E-value: 8.50e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430   25 KVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIISMLKEVIPQLSCP 104
Cdd:PLN02591   1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  105 IALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMNAIVEASEGFIYL 184
Cdd:PLN02591  81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  185 VSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVKILGESESPEQGLKELEF 264
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240


                 ....*....
gi 15235430  265 FTKSLKSAL 273
Cdd:PLN02591 241 LAKSLKAAL 249
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 15-273 1.63e-125

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237285  Cd Length: 258  Bit Score: 357.50  E-value: 1.63e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430   15 ETFARLKSQGKVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIISML 94
Cdd:PRK13111   1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430   95 KEV-IPQLSCPIALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMNA 173
Cdd:PRK13111  81 REIrEKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  174 IVEASEGFIYLVSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEwGADGVIVGSAMVKILGESe 253
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAA-VADGVIVGSALVKIIEEN- 238

                        250       260
                 ....*....|....*....|
gi 15235430  254 spEQGLKELEFFTKSLKSAL 273
Cdd:PRK13111 239 --PEALEALAAFVKELKAAL 256
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 13-273 6.16e-125

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: 356.30  E-value: 6.16e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  13 LSETFARLKSQGKVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIIS 92
Cdd:COG0159   3 IDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  93 MLKEVIPQLSCPIALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMN 172
Cdd:COG0159  83 LVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIK 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430 173 AIVEASEGFIYLVSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWgADGVIVGSAMVKILGES 252
Cdd:COG0159 163 KIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLIEEG 241

                       250       260
                ....*....|....*....|.
gi 15235430 253 EsPEQGLKELEFFTKSLKSAL 273
Cdd:COG0159 242 G-DDEALEALAAFVRELKAAL 261
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 27-270 1.88e-118

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: 339.07  E-value: 1.88e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  27 ALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIISMLKEVIPQLSCPIA 106
Cdd:cd04724   1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430 107 LFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMNAIVEASEGFIYLVS 186
Cdd:cd04724  81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430 187 SVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWgADGVIVGSAMVKILGESeSPEQGLKELEFFT 266
Cdd:cd04724 161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEG-GEEEALEALKELA 238


                ....
gi 15235430 267 KSLK 270
Cdd:cd04724 239 ESLK 242
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
17-273 3.14e-112

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 323.88  E-value: 3.14e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430    17 FARLKSQGKVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIISMLKE 96
Cdd:pfam00290   1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430    97 V-IPQLSCPIALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMNAIV 175
Cdd:pfam00290  81 VrSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430   176 EASEGFIYLVSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAeWGADGVIVGSAMVKILGES-ES 254
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAA-AGADGVIVGSALVRIIEEAaDG 239

                         250
                  ....*....|....*....
gi 15235430   255 PEQGLKELEFFTKSLKSAL 273
Cdd:pfam00290 240 PEQGLARLEELAGEMKAAA 258
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 17-270 1.40e-106

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: 309.66  E-value: 1.40e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430    17 FARLKSQGKVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIISMLKE 96
Cdd:TIGR00262   1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430    97 VIPQL-SCPIALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMNAIV 175
Cdd:TIGR00262  81 VRQKHpNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430   176 EASEGFIYLVSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVKILGES-ES 254
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIEENlNT 240

                         250
                  ....*....|....*.
gi 15235430   255 PEQGLKELEFFTKSLK 270
Cdd:TIGR00262 241 PEKMLQALEEFVQNLK 256
trpA CHL00200
tryptophan synthase alpha subunit; Provisional
 13-275 4.58e-106

tryptophan synthase alpha subunit; Provisional


Pssm-ID: 214394  Cd Length: 263  Bit Score: 308.62  E-value: 4.58e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430   13 LSETFARLKSQgkVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIIS 92
Cdd:CHL00200   4 ISNVFEKLDKQ--CALIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNKILS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430   93 MLKEVIPQLSCPIALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMN 172
Cdd:CHL00200  82 ILSEVNGEIKAPIVIFTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAPTSSKSRIQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  173 AIVEASEGFIYLVSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVKILgES 252
Cdd:CHL00200 162 KIARAAPGCIYLVSTTGVTGLKTELDKKLKKLIETIKKMTNKPIILGFGISTSEQIKQIKGWNINGIVIGSACVQIL-LG 240

                        250       260
                 ....*....|....*....|...
gi 15235430  253 ESPEQGLKELEFFTKSLKSALVS 275
Cdd:CHL00200 241 SSPEKGLDQLSEFCKVAKKSIIS 263
trpA PRK13125
tryptophan synthase subunit alpha; Provisional
 27-273 1.41e-28

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237286  Cd Length: 244  Bit Score: 109.36  E-value: 1.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430   27 ALIPYITAGDPDLSTTAKALKVLDSCgSDIIELGVPYSDPLADGPAIqaaaRRSLLKGTNfNSIISMLKEVIPQLSCPIA 106
Cdd:PRK13125   5 GLVVYLTAGYPNVESFKEFIIGLVEL-VDILELGIPPKYPKYDGPVI----RKSHRKVKG-LDIWPLLEEVRKDVSVPII 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  107 LFTYYNPILRRgVENYMTVIKNAGVHGLLVPDVPL---EETETLRNEARKHQIELVLLTTPTTPKERMNAIVEASEGFIY 183
Cdd:PRK13125  79 LMTYLEDYVDS-LDNFLNMARDVGADGVLFPDLLIdypDDLEKYVEIIKNKGLKPVFFTSPKFPDLLIHRLSKLSPLFIY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430  184 LvssvGV---TGTRESVNekVQSLLQQIKE-ATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVKILGESespeqGL 259
Cdd:PRK13125 158 Y----GLrpaTGVPLPVS--VERNIKRVRNlVGNKYLVVGFGLDSPEDARDALSAGADGVVVGTAFIEELEKN-----GV 226

                        250
                 ....*....|....
gi 15235430  260 KELEFFTKSLKSAL 273
Cdd:PRK13125 227 ESALNLLKKIRGAL 240
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 125-243 3.67e-10

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: 57.98  E-value: 3.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430 125 VIKNAGVHGLLVPDVPL---EETETLRNEARKH--QIELVLLTTPTTPKERMnAIVEASEGFIYLVSSVGVTGTREsVNE 199
Cdd:cd04722  79 AARAAGADGVEIHGAVGylaREDLELIRELREAvpDVKVVVKLSPTGELAAA-AAEEAGVDEVGLGNGGGGGGGRD-AVP 156

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15235430 200 KVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGS 243
Cdd:cd04722 157 IADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 184-245 1.74e-06

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: 47.86  E-value: 1.74e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15235430   184 LVSSVGVTGTRESVNEKvqsLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAM 245
Cdd:pfam00977 164 LLTDIDRDGTLSGPDLE---LTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSAL 222
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 172-244 4.16e-06

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: 46.41  E-value: 4.16e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15235430 172 NAIVEASEGFIYLVSS-VGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSA 244
Cdd:cd04729 135 EALNAAKLGFDIIGTTlSGYTEETAKTEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSA 208
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 183-245 6.63e-06

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: 46.11  E-value: 6.63e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15235430 183 YLVSSVGVTGTRESVNEkvqSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAM 245
Cdd:cd04723 162 LIVLDIDRVGSGQGPDL---ELLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASAL 221
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 183-244 8.55e-06

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: 45.80  E-value: 8.55e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15235430 183 YLVSSVGVTGTRESVNEKvqsLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSA 244
Cdd:COG0106 162 ILYTDISRDGTLQGPNLE---LYRELAAATGIPVIASGGVSSLDDLRALKELGVEGAIVGKA 220
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
189-244 2.96e-05

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 43.98  E-value: 2.96e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15235430  189 GVTGTRESVNEKVQSLLQQIKEATSKPV-AVGfGISKPEHVKQVAEWGADGVIVGSA 244
Cdd:PRK01130 149 GYTEETKKPEEPDFALLKELLKAVGCPViAEG-RINTPEQAKKALELGAHAVVVGGA 204
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
 221-262 3.41e-05

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: 43.99  E-value: 3.41e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 15235430 221 GISKPEHVKQVAEWGADGVIVGSAMVKilgeSESPEQGLKEL 262
Cdd:cd00331 180 GISTPEDVKRLAEAGADAVLIGESLMR----APDPGAALREL 217
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 191-247 4.55e-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: 43.62  E-value: 4.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15235430   191 TGTREsvNEKVQ-SLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVK 247
Cdd:pfam00977  52 DAAKE--GRPVNlDVVEEIAEEVFIPVQVGGGIRSLEDVERLLSAGADRVIIGTAAVK 107
trpC PRK00278
indole-3-glycerol phosphate synthase TrpC;
221-262 1.45e-04

indole-3-glycerol phosphate synthase TrpC;


Pssm-ID: 234710  Cd Length: 260  Bit Score: 42.07  E-value: 1.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 15235430  221 GISKPEHVKQVAEWGADGVIVGSAMVKilgeSESPEQGLKEL 262
Cdd:PRK00278 219 GIFTPEDLKRLAKAGADAVLVGESLMR----ADDPGAALREL 256
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 183-244 1.73e-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: 41.70  E-value: 1.73e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15235430 183 YLVSSVGVTGTRESVNEkvqSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSA 244
Cdd:cd04732 163 IIYTDISRDGTLSGPNF---ELYKELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKA 221
ThiG pfam05690
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
 204-244 7.74e-04

Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole biosynthesis protein G sequences. ThiG, together with ThiF and ThiH, is proposed to be involved in the synthesis of 4-methyl-5-(b-hydroxyethyl)thiazole (THZ) which is an intermediate in the thiazole production pathway. This family also includes triosephosphate isomerase and pyridoxal 5'-phosphate synthase subunit PdxS.


Pssm-ID: 428589  Cd Length: 247  Bit Score: 39.93  E-value: 7.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 15235430   204 LLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSA 244
Cdd:pfam05690 166 NLKIIIEEADVPVIVDAGIGTPSDAAQAMELGADAVLLNTA 206
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 193-263 7.85e-04

The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 40.44  E-value: 7.85e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15235430 193 TRESV--------NEKVQSLLQQIKEATSKPVavgfgiskpehvkqVAEWGADGVIVGSAMVKILGESESPEQGLKELE 263
Cdd:cd14751 308 TRTSAyespevanNPMVAAFKPALETAVPRPP--------------IPEWGELFEPLTLAFAKVLRGEKSPREALDEAA 372
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 195-247 8.52e-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: 39.64  E-value: 8.52e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15235430 195 ESVNEKVqslLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVK 247
Cdd:COG0106  58 KPVNLEL---IEEIAKATGLPVQVGGGIRSLEDIERLLDAGASRVILGTAAVK 107
ThiG cd04728
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ...
 204-244 1.07e-03

Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH).


Pssm-ID: 240079  Cd Length: 248  Bit Score: 39.39  E-value: 1.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 15235430 204 LLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSA 244
Cdd:cd04728 166 NLRIIIERADVPVIVDAGIGTPSDAAQAMELGADAVLLNTA 206
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 203-246 1.34e-03

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 39.00  E-value: 1.34e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15235430 203 SLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMV 246
Cdd:cd04730 146 ALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFL 189
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 215-262 1.82e-03

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 38.70  E-value: 1.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 15235430  215 PVAVGFGISKPEHVKQVAEWGADGVIVGSAMVKilgeSESPEQGLKEL 262
Cdd:PRK04302 175 KVLCGAGISTGEDVKAALELGADGVLLASGVVK----AKDPEAALRDL 218
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 204-246 2.31e-03

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 38.94  E-value: 2.31e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15235430 204 LLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMV 246
Cdd:COG2070 149 LVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFL 191
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 184-247 2.40e-03

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 38.35  E-value: 2.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15235430  184 LVSSVGVTGTRESVN-EKVQSLLqqikEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVK 247
Cdd:PRK13585 167 LFTNVDVEGLLEGVNtEPVKELV----DSVDIPVIASGGVTTLDDLRALKEAGAAGVVVGSALYK 227
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 179-244 4.07e-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: 4.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15235430   179 EGFIYlvSSVGVTGTRESVNEKvqsLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSA 244
Cdd:TIGR00007 160 EGIIY--TDISRDGTLSGPNFE---LTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKA 220
thiG PRK00208
thiazole synthase; Reviewed
 205-244 4.86e-03

thiazole synthase; Reviewed


Pssm-ID: 234687  Cd Length: 250  Bit Score: 37.73  E-value: 4.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 15235430  205 LQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSA 244
Cdd:PRK00208 167 LRIIIEQADVPVIVDAGIGTPSDAAQAMELGADAVLLNTA 206
BtpA COG0434
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];
202-255 4.96e-03

Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440203  Cd Length: 268  Bit Score: 37.46  E-value: 4.96e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15235430 202 QSLLQQIKEAT-SKPVAVGFGIsKPEHVKQVAEWgADGVIVGSAMvKILGESESP 255
Cdd:COG0434 200 LEDLKRVKEAApDVPVLVGSGV-TPENVAELLSV-ADGAIVGSSL-KRDGKTWNP 251
PRK07695 PRK07695
thiazole tautomerase TenI;
203-270 6.00e-03

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 36.92  E-value: 6.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15235430  203 SLLQQIKEATSKPV-AVGfGIsKPEHVKQVAEWGADGVIVGSAMVkilgeseSPEQGLKELEFFTKSLK 270
Cdd:PRK07695 139 EELSDIARALSIPViAIG-GI-TPENTRDVLAAGVSGIAVMSGIF-------SSANPYSKAKRYAESIK 198
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 183-245 6.37e-03

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 37.25  E-value: 6.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15235430  183 YLVSSVGVTGTRESVNekvQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEW---GADGVIVGSAM 245
Cdd:PRK14024 163 YVVTDVTKDGTLTGPN---LELLREVCARTDAPVVASGGVSSLDDLRALAELvplGVEGAIVGKAL 225
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 184-263 7.55e-03

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 36.69  E-value: 7.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235430 184 LVSSV--GVTGTR--ESVNEKVQSLLQQIKEAT-SKPVAVGFGIsKPEHVKQVAEWGADGVIVGSAMVKilgeSESPEQG 258
Cdd:cd00429 132 LVMSVnpGFGGQKfiPEVLEKIRKLRELIPENNlNLLIEVDGGI-NLETIPLLAEAGADVLVAGSALFG----SDDYAEA 206


                ....*
gi 15235430 259 LKELE 263
Cdd:cd00429 207 IKELR 211
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 195-247 8.27e-03

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 36.58  E-value: 8.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15235430  195 ESVNEKvqsLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVK 247
Cdd:PRK00748  59 KPVNLE---LIEAIVKAVDIPVQVGGGIRSLETVEALLDAGVSRVIIGTAAVK 108
 
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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