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Conserved domains on  [gi|544991675|ref|WP_021388541|]
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gamma-glutamyl-gamma-aminobutyrate hydrolase family protein [Clostridioides difficile]

Protein Classification

gamma-glutamyl-gamma-aminobutyrate hydrolase family protein( domain architecture ID 11449689)

gamma-glutamyl-gamma-aminobutyrate hydrolase family protein may catalyze the hydrolysis of the gamma-glutamyl linkage of gamma-glutamyl-gamma-aminobutyrate, an important step in putrescine degradation

CATH:  3.40.50.880
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0016811
MEROPS:  C26
PubMed:  11517925|15590624

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 14-248 3.32e-106

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


:

Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 306.32  E-value: 3.32e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  14 ISGNLLIDEGgmfpgYERAYVNNDYIQSVVMCKAIPYIVPIVYDDEIIKEQVSNIDALILSGGQDVNPLIWKEEPHNKLE 93
Cdd:COG2071    1 ITADLRTAGG-----YPAHYLPEDYVRAVRAAGGLPVLLPPVGDEEDLDELLDRLDGLVLTGGADVDPALYGEEPHPELG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  94 AISPKRDSFDMKLLKHALDMKKPVLGICRGEQIINVTEGGSLYQDLSLIEGAYIKHNQQHLSNVPTHTVQIKEGTKLYEI 173
Cdd:COG2071   76 PIDPERDAFELALIRAALERGKPVLGICRGMQLLNVALGGTLYQDLPDQVPGALDHRQPAPRYAPRHTVEIEPGSRLARI 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544991675 174 LGEKEVLVNSFHHLVVNKVAPGYIVSATSKDGLIEAIEKEGSEFVIGIQWHPEMMTRDYDNMKKIFMAIVKEASK 248
Cdd:COG2071  156 LGEEEIRVNSLHHQAVKRLGPGLRVSARAPDGVIEAIESPGAPFVLGVQWHPEWLAASDPLSRRLFEAFVEAARA 230
 
Name Accession Description Interval E-value
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 14-248 3.32e-106

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 306.32  E-value: 3.32e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  14 ISGNLLIDEGgmfpgYERAYVNNDYIQSVVMCKAIPYIVPIVYDDEIIKEQVSNIDALILSGGQDVNPLIWKEEPHNKLE 93
Cdd:COG2071    1 ITADLRTAGG-----YPAHYLPEDYVRAVRAAGGLPVLLPPVGDEEDLDELLDRLDGLVLTGGADVDPALYGEEPHPELG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  94 AISPKRDSFDMKLLKHALDMKKPVLGICRGEQIINVTEGGSLYQDLSLIEGAYIKHNQQHLSNVPTHTVQIKEGTKLYEI 173
Cdd:COG2071   76 PIDPERDAFELALIRAALERGKPVLGICRGMQLLNVALGGTLYQDLPDQVPGALDHRQPAPRYAPRHTVEIEPGSRLARI 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544991675 174 LGEKEVLVNSFHHLVVNKVAPGYIVSATSKDGLIEAIEKEGSEFVIGIQWHPEMMTRDYDNMKKIFMAIVKEASK 248
Cdd:COG2071  156 LGEEEIRVNSLHHQAVKRLGPGLRVSARAPDGVIEAIESPGAPFVLGVQWHPEWLAASDPLSRRLFEAFVEAARA 230
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 10-226 3.56e-89

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 262.96  E-value: 3.56e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675   10 PIIGISGNLLIDEGGMFPGYERAYVNNDYIQSVVMCKAIPYIVPIVYDDEIIKEQVSNIDALILSGGQDVNPLIWKEEPH 89
Cdd:pfam07722   1 PVIGITANEESLGGHVFHGAGESYLAAGYVEAVEGAGGLPVLLPILGDPEDAAAILDRLDGLLLTGGPNVDPHFYGEEPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675   90 NKLEAISPKRDSFDMKLLKHALDMKKPVLGICRGEQIINVTEGGSLYQDLSLIEG--AYIKHNQQHLSNvPTHTVQIKEG 167
Cdd:pfam07722  81 ESGGPYDPARDAYELALIRAALARGKPILGICRGFQLLNVALGGTLYQDIQEQPGftDHREHCQVAPYA-PSHAVNVEPG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  168 TKLYEILGEKEVLVNSFHHLVVNKVAPGYIVSATSKDGLIEAIEKEGSE-FVIGIQWHPE 226
Cdd:pfam07722 160 SLLASLLGSEEFRVNSLHHQAIDRLAPGLRVEAVAPDGTIEAIESPNAKgFALGVQWHPE 219
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 12-243 9.60e-78

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 232.85  E-value: 9.60e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  12 IGISGNLLIDEGGMFPgyeRAYVNNDYIQSVVMCKAIPYIVPIVYDDEIIKEQVSNIDALILSGGQDVNPLIWKEEPHNK 91
Cdd:cd01745    1 IGITARLREEEGGYER---RDYLNQYYVDAVRKAGGLPVLLPPVDDEEDLEQYLELLDGLLLTGGGDVDPPLYGEEPHPE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  92 LEAISPKRDSFDMKLLKHALDMKKPVLGICRGEQIINVTEGGSLYQDLSliegayikhnqqhlsnvpthtvqikegtkly 171
Cdd:cd01745   78 LGPIDPERDAFELALLRAALERGKPILGICRGMQLLNVALGGTLYQDIR------------------------------- 126

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544991675 172 eilgekevlVNSFHHLVVNKVAPGYIVSATSKDGLIEAIEKEGSEFVIGIQWHPEMMTRDYDNMKKIFMAIV 243
Cdd:cd01745  127 ---------VNSLHHQAIKRLADGLRVEARAPDGVIEAIESPDRPFVLGVQWHPEWLADTDPDSLKLFEAFV 189
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 28-232 3.91e-29

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 109.99  E-value: 3.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  28 GYERAYVNNDYIQSVVMCKAIPYIVP-IVYDDEIIKEQVSNIDALILSGG-QDVNPLIWKE---EPhnkleAISPKRDSF 102
Cdd:PRK11366  21 GHATQTLQEKYLNAIIHAGGLPIALPhALAEPSLLEQLLPKLDGIYLPGSpSNVQPHLYGEngdEP-----DADPGRDLL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 103 DMKLLKHALDMKKPVLGICRGEQIINVTEGGSLYQDLsLIEGAYIKHNQQHLSNV-----PTHTVQIKEGTKLYEILGE- 176
Cdd:PRK11366  96 SMALINAALERRIPIFAICRGLQELVVATGGSLHRKL-CEQPELLEHREDPELPVeqqyaPSHEVQVEEGGLLSALLPEc 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544991675 177 KEVLVNSFHHLVVNKVAPGYIVSATSKDGLIEAIEKEGSEFVIGIQWHPEMMTRDY 232
Cdd:PRK11366 175 SNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEY 230
 
Name Accession Description Interval E-value
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 14-248 3.32e-106

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 306.32  E-value: 3.32e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  14 ISGNLLIDEGgmfpgYERAYVNNDYIQSVVMCKAIPYIVPIVYDDEIIKEQVSNIDALILSGGQDVNPLIWKEEPHNKLE 93
Cdd:COG2071    1 ITADLRTAGG-----YPAHYLPEDYVRAVRAAGGLPVLLPPVGDEEDLDELLDRLDGLVLTGGADVDPALYGEEPHPELG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  94 AISPKRDSFDMKLLKHALDMKKPVLGICRGEQIINVTEGGSLYQDLSLIEGAYIKHNQQHLSNVPTHTVQIKEGTKLYEI 173
Cdd:COG2071   76 PIDPERDAFELALIRAALERGKPVLGICRGMQLLNVALGGTLYQDLPDQVPGALDHRQPAPRYAPRHTVEIEPGSRLARI 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544991675 174 LGEKEVLVNSFHHLVVNKVAPGYIVSATSKDGLIEAIEKEGSEFVIGIQWHPEMMTRDYDNMKKIFMAIVKEASK 248
Cdd:COG2071  156 LGEEEIRVNSLHHQAVKRLGPGLRVSARAPDGVIEAIESPGAPFVLGVQWHPEWLAASDPLSRRLFEAFVEAARA 230
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 10-226 3.56e-89

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 262.96  E-value: 3.56e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675   10 PIIGISGNLLIDEGGMFPGYERAYVNNDYIQSVVMCKAIPYIVPIVYDDEIIKEQVSNIDALILSGGQDVNPLIWKEEPH 89
Cdd:pfam07722   1 PVIGITANEESLGGHVFHGAGESYLAAGYVEAVEGAGGLPVLLPILGDPEDAAAILDRLDGLLLTGGPNVDPHFYGEEPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675   90 NKLEAISPKRDSFDMKLLKHALDMKKPVLGICRGEQIINVTEGGSLYQDLSLIEG--AYIKHNQQHLSNvPTHTVQIKEG 167
Cdd:pfam07722  81 ESGGPYDPARDAYELALIRAALARGKPILGICRGFQLLNVALGGTLYQDIQEQPGftDHREHCQVAPYA-PSHAVNVEPG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  168 TKLYEILGEKEVLVNSFHHLVVNKVAPGYIVSATSKDGLIEAIEKEGSE-FVIGIQWHPE 226
Cdd:pfam07722 160 SLLASLLGSEEFRVNSLHHQAIDRLAPGLRVEAVAPDGTIEAIESPNAKgFALGVQWHPE 219
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 12-243 9.60e-78

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 232.85  E-value: 9.60e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  12 IGISGNLLIDEGGMFPgyeRAYVNNDYIQSVVMCKAIPYIVPIVYDDEIIKEQVSNIDALILSGGQDVNPLIWKEEPHNK 91
Cdd:cd01745    1 IGITARLREEEGGYER---RDYLNQYYVDAVRKAGGLPVLLPPVDDEEDLEQYLELLDGLLLTGGGDVDPPLYGEEPHPE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  92 LEAISPKRDSFDMKLLKHALDMKKPVLGICRGEQIINVTEGGSLYQDLSliegayikhnqqhlsnvpthtvqikegtkly 171
Cdd:cd01745   78 LGPIDPERDAFELALLRAALERGKPILGICRGMQLLNVALGGTLYQDIR------------------------------- 126

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544991675 172 eilgekevlVNSFHHLVVNKVAPGYIVSATSKDGLIEAIEKEGSEFVIGIQWHPEMMTRDYDNMKKIFMAIV 243
Cdd:cd01745  127 ---------VNSLHHQAIKRLADGLRVEARAPDGVIEAIESPDRPFVLGVQWHPEWLADTDPDSLKLFEAFV 189
puuD PRK11366
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional
 28-232 3.91e-29

gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional


Pssm-ID: 183101 [Multi-domain]  Cd Length: 254  Bit Score: 109.99  E-value: 3.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  28 GYERAYVNNDYIQSVVMCKAIPYIVP-IVYDDEIIKEQVSNIDALILSGG-QDVNPLIWKE---EPhnkleAISPKRDSF 102
Cdd:PRK11366  21 GHATQTLQEKYLNAIIHAGGLPIALPhALAEPSLLEQLLPKLDGIYLPGSpSNVQPHLYGEngdEP-----DADPGRDLL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 103 DMKLLKHALDMKKPVLGICRGEQIINVTEGGSLYQDLsLIEGAYIKHNQQHLSNV-----PTHTVQIKEGTKLYEILGE- 176
Cdd:PRK11366  96 SMALINAALERRIPIFAICRGLQELVVATGGSLHRKL-CEQPELLEHREDPELPVeqqyaPSHEVQVEEGGLLSALLPEc 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544991675 177 KEVLVNSFHHLVVNKVAPGYIVSATSKDGLIEAIEKEGSEFVIGIQWHPEMMTRDY 232
Cdd:PRK11366 175 SNFWVNSLHGQGAKVVSPRLRVEARSPDGLVEAVSVINHPFALGVQWHPEWNSSEY 230
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 23-227 3.03e-16

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 74.98  E-value: 3.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  23 GGMFPGYERAYVNNDYIQSVVMCkaipyivpiVYDDEIIKEQVS--NIDALILSGG-QDVNPliwkEEPHNKLEaispkr 99
Cdd:COG0518   11 GGQYPGLIARRLREAGIELDVLR---------VYAGEILPYDPDleDPDGLILSGGpMSVYD----EDPWLEDE------ 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 100 dsfdMKLLKHALDMKKPVLGICRGEQIINVTEGGSLYQdlsliegayikhnqqhlSNVP---THTVQIKEGTKLYEILGE 176
Cdd:COG0518   72 ----PALIREAFELGKPVLGICYGAQLLAHALGGKVEP-----------------GPGReigWAPVELTEADPLFAGLPD 130

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 544991675 177 KEVLVNSfHHLVVNKVAPGYIVSATSKDGLIEAIEKEGSefVIGIQWHPEM 227
Cdd:COG0518  131 EFTVWMS-HGDTVTELPEGAEVLASSDNCPNQAFRYGRR--VYGVQFHPEV 178
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 43-226 6.09e-12

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 62.17  E-value: 6.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  43 VMCKAIPYIVPIvyddEIIKEqvSNIDALILSGGqdvnpliwkeePHNKLEAISPkrdSFDMKLLkhalDMKKPVLGICR 122
Cdd:cd01742   23 VYSEILPNTTPL----EEIKL--KNPKGIILSGG-----------PSSVYEEDAP---RVDPEIF----ELGVPVLGICY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 123 GEQIINVTEGGSLyqdlsliegayikhnqqHLSNVP---THTVQIKEGTKLYEILGEKEVLVNSfHHLVVNKVAPGYIVS 199
Cdd:cd01742   79 GMQLIAKALGGKV-----------------ERGDKReygKAEIEIDDSSPLFEGLPDEQTVWMS-HGDEVVKLPEGFKVI 140

                        170       180
                 ....*....|....*....|....*..
gi 544991675 200 ATSKDGLIEAIEKEGSEFvIGIQWHPE 226
Cdd:cd01742  141 ASSDNCPVAAIANEEKKI-YGVQFHPE 166
GATase pfam00117
Glutamine amidotransferase class-I;
51-226 1.80e-10

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 58.40  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675   51 IVPIVYDDEIIKEQvsNIDALILSGGQDvnpliwkeephnkleaiSPKRDSFDMKLLKHALDMKKPVLGICRGEQIINVT 130
Cdd:pfam00117  26 VVPNDTPAEEILEE--NPDGIILSGGPG-----------------SPGAAGGAIEAIREARELKIPILGICLGHQLLALA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  131 EGGSLYQdlsLIEGAYIKHNQQhlsnvpthtvQIKEGTKLYEILGeKEVLVNSFHHLVVNK--VAPGYIVSATS-KDGLI 207
Cdd:pfam00117  87 FGGKVVK---AKKFGHHGKNSP----------VGDDGCGLFYGLP-NVFIVRRYHSYAVDPdtLPDGLEVTATSeNDGTI 152

                         170
                  ....*....|....*....
gi 544991675  208 EAIEKEGSEFvIGIQWHPE 226
Cdd:pfam00117 153 MGIRHKKLPI-FGVQFHPE 170
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 47-226 5.61e-09

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 54.17  E-value: 5.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  47 AIPYIVPIVYDDEIIKEqVSNIDALILSGG-QDVNpliwkEEPHNKLEAIspkrdsfdMKLLKHALDMKKPVLGICRGEQ 125
Cdd:cd01741   27 TIEIDVVDVYAGELLPD-LDDYDGLVILGGpMSVD-----EDDYPWLKKL--------KELIRQALAAGKPVLGICLGHQ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 126 IINVTEGGSLYQDLSLIEGAyikhnqqhlsnvpTHTVQIKEGTKLYEILGE--KEVLVNSFHHLVVNKVAPGYIVSATSK 203
Cdd:cd01741   93 LLARALGGKVGRNPKGWEIG-------------WFPVTLTEAGKADPLFAGlpDEFPVFHWHGDTVVELPPGAVLLASSE 159

                        170       180
                 ....*....|....*....|...
gi 544991675 204 DGLIEAIEKEGseFVIGIQWHPE 226
Cdd:cd01741  160 ACPNQAFRYGD--RALGLQFHPE 180
guaA PRK00074
GMP synthase; Reviewed
 51-226 1.86e-08

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 54.28  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  51 IVPIVYDDEIIKEQvsNIDALILSGGqdvnpliwkeePHNKLEAISPKRDsfdmkllKHALDMKKPVLGICRGEQIINVT 130
Cdd:PRK00074  32 IVPYDISAEEIRAF--NPKGIILSGG-----------PASVYEEGAPRAD-------PEIFELGVPVLGICYGMQLMAHQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 131 EGGSLyqdlsliegayikhnqqhlsnVPTHT-------VQIKEGTKLYEILGEKEVLVNSfHHLVVNKVAPGYIVSATSK 203
Cdd:PRK00074  92 LGGKV---------------------ERAGKreygraeLEVDNDSPLFKGLPEEQDVWMS-HGDKVTELPEGFKVIASTE 149

                        170       180
                 ....*....|....*....|...
gi 544991675 204 DGLIEAIEKEGSEFViGIQWHPE 226
Cdd:PRK00074 150 NCPIAAIANEERKFY-GVQFHPE 171
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
52-246 4.94e-08

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 53.18  E-value: 4.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  52 VPIVYDDEIIKEQVS--NIDALILSGGQDvnpliwkeephnkleaiSPKRDSFDMKLLKHALDmKKPVLGICRGEQIINV 129
Cdd:PRK14607  27 IEVVRNDEITIEEIEalNPSHIVISPGPG-----------------RPEEAGISVEVIRHFSG-KVPILGVCLGHQAIGY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 130 TEGGSLYQDLSLIEG--AYIKHNqqhlsnvpthtvqikeGTKLYEILGEKEVLVNsFHHLVVNKVA-PG-YIVSATSKDG 205
Cdd:PRK14607  89 AFGGKIVHAKRILHGktSPIDHN----------------GKGLFRGIPNPTVATR-YHSLVVEEASlPEcLEVTAKSDDG 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 544991675 206 LIEAIEKEgsEFVI-GIQWHPE-MMTRDYDNMKKIFMAIVKEA 246
Cdd:PRK14607 152 EIMGIRHK--EHPIfGVQFHPEsILTEEGKRILKNFLNYQREE 192
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 53-226 1.99e-07

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 49.84  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  53 PIVYD-DEIIKEQV--SNIDALILSGGqdvnpliwkeePHNkleaisPKRDSFDMKLLKHaLDMKKPVLGICRGEQIINV 129
Cdd:cd01743   25 VVVVRnDEITLEELelLNPDAIVISPG-----------PGH------PEDAGISLEIIRA-LAGKVPILGVCLGHQAIAE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 130 TEGGslyqdlSLIEGAYIKHNQQHLSnvpTHTvqikeGTKLYEILGEkEVLVNSFHHLVVNKVAPGY--IVSATSKDGLI 207
Cdd:cd01743   87 AFGG------KVVRAPEPMHGKTSEI---HHD-----GSGLFKGLPQ-PFTVGRYHSLVVDPDPLPDllEVTASTEDGVI 151

                        170
                 ....*....|....*....
gi 544991675 208 EAIEKEgSEFVIGIQWHPE 226
Cdd:cd01743  152 MALRHR-DLPIYGVQFHPE 169
PLN02347 PLN02347
GMP synthetase
 70-228 7.64e-07

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 49.30  E-value: 7.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  70 ALILSGGqdvnpliwkeePHNKLEAISPkrdSFDMKLLKHALDMKKPVLGICRGEQIINVTEGGSLYQDLSlieGAYIKH 149
Cdd:PLN02347  56 VVILSGG-----------PHSVHVEGAP---TVPEGFFDYCRERGVPVLGICYGMQLIVQKLGGEVKPGEK---QEYGRM 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 150 NqqhlsnvpthtVQIKEGTKLYEILG-EKEVLVNSFHHLVVNKVAPGYIVSATSKDGLIEAIEKEGSEFvIGIQWHPEMM 228
Cdd:PLN02347 119 E-----------IRVVCGSQLFGDLPsGETQTVWMSHGDEAVKLPEGFEVVAKSVQGAVVAIENRERRI-YGLQYHPEVT 186
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 52-226 8.78e-07

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 47.82  E-value: 8.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  52 VPIVYDDEIIKEQVSNI--DALILSGGqdvnpliwkeePHNKLEA-ISPKrdsfdmkLLKHaLDMKKPVLGICRGEQIIN 128
Cdd:PRK05670  26 VVVYRNDEITLEEIEALnpDAIVLSPG-----------PGTPAEAgISLE-------LIRE-FAGKVPILGVCLGHQAIG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 129 VTEGGslyqdlSLIEGAYIKHNQQhlSNVpTHTvqikeGTKLYEILGEkEVLVNSFHHLVVNK--VAPGYIVSATSKDGL 206
Cdd:PRK05670  87 EAFGG------KVVRAKEIMHGKT--SPI-EHD-----GSGIFAGLPN-PFTVTRYHSLVVDResLPDCLEVTAWTDDGE 151

                        170       180
                 ....*....|....*....|
gi 544991675 207 IEAIEKEgSEFVIGIQWHPE 226
Cdd:PRK05670 152 IMGVRHK-ELPIYGVQFHPE 170
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 53-226 2.79e-06

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 46.57  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  53 PIVYD-DEIIKEQVS--NIDALILSGGqdvnpliwkeePHNKLEA-ISpkrdsfdMKLLKHALDmKKPVLGICRGEQIIN 128
Cdd:COG0512   25 VVVVRnDEITLEEIEalAPDGIVLSPG-----------PGTPEEAgIS-------LEVIRAFAG-KIPILGVCLGHQAIG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 129 VTEGGSLYQdlslieGAYIKHNQQhlSNVpTHTvqikeGTKLYEILgEKEVLVNSFHHLVVNK--VAPGYIVSATSKDGL 206
Cdd:COG0512   86 EAFGGKVVR------APEPMHGKT--SPI-THD-----GSGLFAGL-PNPFTATRYHSLVVDRetLPDELEVTAWTEDGE 150

                        170       180
                 ....*....|....*....|.
gi 544991675 207 IEAIE-KEGSefVIGIQWHPE 226
Cdd:COG0512  151 IMGIRhRELP--IEGVQFHPE 169
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 51-130 9.03e-06

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 43.74  E-value: 9.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  51 IVPIVYDDEIIKEQVSNIDALILSGGQDVnpliwkeephnkleAISPKRDSFDMKLLKHALDMKKPVLGICRGEQIINVT 130
Cdd:cd01653   30 VVSPDGGPVESDVDLDDYDGLILPGGPGT--------------PDDLARDEALLALLREAAAAGKPILGICLGAQLLVLG 95
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 37-226 9.52e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 44.86  E-value: 9.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  37 DY----IQSVVmcKAIPY--IVPIVYDDeiiKEQVSNIDALILSG----GQDVNPLiwkeephnkleaispKRDSFDmKL 106
Cdd:PRK13181   6 DYgagnLRSVA--NALKRlgVEAVVSSD---PEEIAGADKVILPGvgafGQAMRSL---------------RESGLD-EA 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 107 LKHALDMKKPVLGICRGEQII-NVTEGGSLyQDLSLIEGAYIKHNQQHLSnVPtH----TVQIKEGTKLYEILGEKE--V 179
Cdd:PRK13181  65 LKEHVEKKQPVLGICLGMQLLfESSEEGNV-KGLGLIPGDVKRFRSEPLK-VP-QmgwnSVKPLKESPLFKGIEEGSyfY 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 544991675 180 LVNSFHhlvVNKVAPGYIVsATSKDGLI--EAIEKEGsefVIGIQWHPE 226
Cdd:PRK13181 142 FVHSYY---VPCEDPEDVL-ATTEYGVPfcSAVAKDN---IYAVQFHPE 183
trpG CHL00101
anthranilate synthase component 2
 116-228 3.58e-05

anthranilate synthase component 2


Pssm-ID: 214365 [Multi-domain]  Cd Length: 190  Bit Score: 43.18  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 116 PVLGICRGEQIINVTEGGSLYQDLSLIEG--AYIKHNQQHL-SNVPThtvqikegtklyeilgekEVLVNSFHHLVVNKV 192
Cdd:CHL00101  74 PILGVCLGHQSIGYLFGGKIIKAPKPMHGktSKIYHNHDDLfQGLPN------------------PFTATRYHSLIIDPL 135

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 544991675 193 AP--GYIVSATSKDGLIEAIEKEGSEFVIGIQWHPEMM 228
Cdd:CHL00101 136 NLpsPLEITAWTEDGLIMACRHKKYKMLRGIQFHPESL 173
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 51-127 6.27e-05

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 40.65  E-value: 6.27e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544991675  51 IVPIVYDDEIIKEQVSNIDALILSGGQDVnpliwkeephnkleAISPKRDSFDMKLLKHALDMKKPVLGICRGEQII 127
Cdd:cd03128   30 VVSPDGGPVESDVDLDDYDGLILPGGPGT--------------PDDLAWDEALLALLREAAAAGKPVLGICLGAQLL 92
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 50-136 3.77e-04

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 40.17  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  50 YIVPIVYDDEIIKEqvSNIDALILSGGqdvnpliwkeePHNkleaisPKRDSFDMKLLKHALDMKKPVLGICRGEQIINV 129
Cdd:cd01744   24 TVVPYNTDAEEILK--LDPDGIFLSNG-----------PGD------PALLDEAIKTVRKLLGKKIPIFGICLGHQLLAL 84


                 ....*..
gi 544991675 130 TEGGSLY 136
Cdd:cd01744   85 ALGAKTY 91
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 55-134 5.05e-04

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 40.34  E-value: 5.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675  55 VYDDEIIKEQVSNIDALILSGG-QDvnPLIWKEE-PHnkleaispkrdsFD----MKLLKHALDMKKPVLGICRGEQIIN 128
Cdd:PRK08250  33 VYAGEALPENADGFDLLIVMGGpQS--PRTTREEcPY------------FDskaeQRLINQAIKAGKAVIGVCLGAQLIG 98


                 ....*.
gi 544991675 129 VTEGGS 134
Cdd:PRK08250  99 EALGAK 104
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 106-226 6.00e-04

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 39.79  E-value: 6.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 106 LLKHALDMKKPVLGICRGEQII-NVTEGGSLYQDLSLIEGAYIKHNQQHLSNVPtH----TVQIKEGTKLYEILGEKEVL 180
Cdd:cd01748   63 ALKEAIASGKPFLGICLGMQLLfESSEEGGGTKGLGLIPGKVVRFPASEGLKVP-HmgwnQLEITKESPLFKGIPDGSYF 141

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 544991675 181 --VNSFHhlvVNKVAPGYIVSATSKDGLIEA-IEKEGsefVIGIQWHPE 226
Cdd:cd01748  142 yfVHSYY---APPDDPDYILATTDYGGKFPAaVEKDN---IFGTQFHPE 184
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 105-226 2.36e-03

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 38.10  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544991675 105 KLLKHALDMKKPVLGICRGEQII-------NVTEGgslyqdLSLIEGAYIKHNQQHLSnVPtH----TVQIKEGTKLYEI 173
Cdd:COG0118   64 EAIREAVAGGKPVLGICLGMQLLferseenGDTEG------LGLIPGEVVRFPASDLK-VP-HmgwnTVEIAKDHPLFAG 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 544991675 174 LGEKE--VLVNSFHhlvVNKVAPGYIVsATSKDGL--IEAIEKEGsefVIGIQWHPE 226
Cdd:COG0118  136 IPDGEyfYFVHSYY---VPPDDPEDVV-ATTDYGVpfTAAVERGN---VFGTQFHPE 185
 
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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