NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1463651485|ref|WP_116686648|]
View 

gamma-glutamyl-gamma-aminobutyrate hydrolase family protein [Pelagibaculum spongiae]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 73)

type 1 glutamine amidotransferase (GATase1) family protein

CATH:  3.40.50.880
PubMed:  10387030
SCOP:  3001405

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GAT_1 super family cl00020
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 1-233 1.39e-65

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.


The actual alignment was detected with superfamily member PRK05665:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 240  Bit Score: 203.12  E-value: 1.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485   1 MKIGILQCDDVQEALQLEFGNYPCMFQNLLNQISNDLTWQVYDVRIGEYPEHLDDCDGYISTGSRYGVNDSLAWLEPLEA 80
Cdd:PRK05665    3 LRICILETDVLRPELVAQYQGYGRMFEQLFARQPIAAEFVVYNVVQGDYPADDEKFDAYLVTGSKADSFGTDPWIQTLKT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  81 FVQKAYRAKKPFVGICFGHQLIAKALGGKVDRSEKGWGAGISFNQIVVQTPWMKPQQNGLDLVVSHQDQVVELPENAQVL 160
Cdd:PRK05665   83 YLLKLYERGDKLLGVCFGHQLLALLLGGKAERASQGWGVGIHRYQLAAHAPWMSPAVTELTLLISHQDQVTALPEGATVI 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1463651485 161 AQSSFCLNYMIQIGSSMLGIQGHPEFSRAYSSALTNARRDRIPAHRVREALNSLHADVDDLTMARWILNFLQQ 233
Cdd:PRK05665  163 ASSDFCPFAAYHIGDQVLCFQGHPEFVHDYSRALLDLRQEHLGEEVYSKGVASLAHDHQGTTVAEWMMRFVAQ 235
 
Name Accession Description Interval E-value
PRK05665 PRK05665
amidotransferase; Provisional
 1-233 1.39e-65

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 203.12  E-value: 1.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485   1 MKIGILQCDDVQEALQLEFGNYPCMFQNLLNQISNDLTWQVYDVRIGEYPEHLDDCDGYISTGSRYGVNDSLAWLEPLEA 80
Cdd:PRK05665    3 LRICILETDVLRPELVAQYQGYGRMFEQLFARQPIAAEFVVYNVVQGDYPADDEKFDAYLVTGSKADSFGTDPWIQTLKT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  81 FVQKAYRAKKPFVGICFGHQLIAKALGGKVDRSEKGWGAGISFNQIVVQTPWMKPQQNGLDLVVSHQDQVVELPENAQVL 160
Cdd:PRK05665   83 YLLKLYERGDKLLGVCFGHQLLALLLGGKAERASQGWGVGIHRYQLAAHAPWMSPAVTELTLLISHQDQVTALPEGATVI 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1463651485 161 AQSSFCLNYMIQIGSSMLGIQGHPEFSRAYSSALTNARRDRIPAHRVREALNSLHADVDDLTMARWILNFLQQ 233
Cdd:PRK05665  163 ASSDFCPFAAYHIGDQVLCFQGHPEFVHDYSRALLDLRQEHLGEEVYSKGVASLAHDHQGTTVAEWMMRFVAQ 235
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-233 6.06e-64

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: 198.25  E-value: 6.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485   2 KIGILQCDDvqealqlEFGNYPCMFQNLLNQisNDLTWQVYDVRIGE---YPEHLDDCDGYISTGSRYGVNDSLAWLEPL 78
Cdd:COG0518     1 KILILDHDP-------FGGQYPGLIARRLRE--AGIELDVLRVYAGEilpYDPDLEDPDGLILSGGPMSVYDEDPWLEDE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  79 EAFVQKAYRAKKPFVGICFGHQLIAKALGGKVDRSEkGWGAGISFNQIVVQTPWMKPQQNGLDLVVSHQDQVVELPENAQ 158
Cdd:COG0518    72 PALIREAFELGKPVLGICYGAQLLAHALGGKVEPGP-GREIGWAPVELTEADPLFAGLPDEFTVWMSHGDTVTELPEGAE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1463651485 159 VLAQSSFCLNYMIQIGSSMLGIQGHPEFSRAYSSALTNARRDRIPAHRVReALNSLHADVDDLTMARWILNFLQQ 233
Cdd:COG0518   151 VLASSDNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADELAAEELL-AEASLHDPELREAGRRLLRNFLRE 224
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 2-185 3.25e-53

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: 169.73  E-value: 3.25e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485   2 KIGILQCDDVQEalqlefgnyPCMFQNLLNQI-SNDLTWQVYDVRIGEYPEHLDDCDGYISTGSRYGV-NDSLAWLEPLE 79
Cdd:cd01741     1 RILILQHDTPEG---------PGLFEDLLREAgAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVdEDDYPWLKKLK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  80 AFVQKAYRAKKPFVGICFGHQLIAKALGGKVDRSEKGWGAGISFNQIVVQTPWMKPQQNG---LDLVVSHQDQVVELPEN 156
Cdd:cd01741    72 ELIRQALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGLpdeFPVFHWHGDTVVELPPG 151

                         170       180
                  ....*....|....*....|....*....
gi 1463651485 157 AQVLAQSSFCLNYMIQIGSSMLGIQGHPE 185
Cdd:cd01741   152 AVLLASSEACPNQAFRYGDRALGLQFHPE 180
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 83-185 1.14e-17

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 77.74  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  83 QKAYRAKKPFVGICFGHQLIAKALGGKVDRSEKG---------WGAGISFNQI-VVQTPWMkpqqngldlvvSHQDQVVE 152
Cdd:TIGR00888  64 EKIFELGVPVLGICYGMQLMAKQLGGEVGRAEKReygkaeleiLDEDDLFRGLpDESTVWM-----------SHGDKVKE 132

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1463651485 153 LPENAQVLAQSSFCLNYMIQIGSSML-GIQGHPE 185
Cdd:TIGR00888 133 LPEGFKVLATSDNCPVAAMAHEEKPIyGVQFHPE 166
GATase pfam00117
Glutamine amidotransferase class-I;
73-187 2.92e-10

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 57.63  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  73 AWLEPLEAFVQKAYRAKKPFVGICFGHQLIAKALGGKVDRSEK----GWgagisfNQIVVQTPWMKPQQNGLDLVVS--H 146
Cdd:pfam00117  54 GAAGGAIEAIREARELKIPILGICLGHQLLALAFGGKVVKAKKfghhGK------NSPVGDDGCGLFYGLPNVFIVRryH 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1463651485 147 QDQVVE--LPENAQVLAQSSFCLNYM--IQIGSSMLGIQGHPEFS 187
Cdd:pfam00117 128 SYAVDPdtLPDGLEVTATSENDGTIMgiRHKKLPIFGVQFHPESI 172
 
Name Accession Description Interval E-value
PRK05665 PRK05665
amidotransferase; Provisional
 1-233 1.39e-65

amidotransferase; Provisional


Pssm-ID: 168162 [Multi-domain]  Cd Length: 240  Bit Score: 203.12  E-value: 1.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485   1 MKIGILQCDDVQEALQLEFGNYPCMFQNLLNQISNDLTWQVYDVRIGEYPEHLDDCDGYISTGSRYGVNDSLAWLEPLEA 80
Cdd:PRK05665    3 LRICILETDVLRPELVAQYQGYGRMFEQLFARQPIAAEFVVYNVVQGDYPADDEKFDAYLVTGSKADSFGTDPWIQTLKT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  81 FVQKAYRAKKPFVGICFGHQLIAKALGGKVDRSEKGWGAGISFNQIVVQTPWMKPQQNGLDLVVSHQDQVVELPENAQVL 160
Cdd:PRK05665   83 YLLKLYERGDKLLGVCFGHQLLALLLGGKAERASQGWGVGIHRYQLAAHAPWMSPAVTELTLLISHQDQVTALPEGATVI 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1463651485 161 AQSSFCLNYMIQIGSSMLGIQGHPEFSRAYSSALTNARRDRIPAHRVREALNSLHADVDDLTMARWILNFLQQ 233
Cdd:PRK05665  163 ASSDFCPFAAYHIGDQVLCFQGHPEFVHDYSRALLDLRQEHLGEEVYSKGVASLAHDHQGTTVAEWMMRFVAQ 235
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-233 6.06e-64

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: 198.25  E-value: 6.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485   2 KIGILQCDDvqealqlEFGNYPCMFQNLLNQisNDLTWQVYDVRIGE---YPEHLDDCDGYISTGSRYGVNDSLAWLEPL 78
Cdd:COG0518     1 KILILDHDP-------FGGQYPGLIARRLRE--AGIELDVLRVYAGEilpYDPDLEDPDGLILSGGPMSVYDEDPWLEDE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  79 EAFVQKAYRAKKPFVGICFGHQLIAKALGGKVDRSEkGWGAGISFNQIVVQTPWMKPQQNGLDLVVSHQDQVVELPENAQ 158
Cdd:COG0518    72 PALIREAFELGKPVLGICYGAQLLAHALGGKVEPGP-GREIGWAPVELTEADPLFAGLPDEFTVWMSHGDTVTELPEGAE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1463651485 159 VLAQSSFCLNYMIQIGSSMLGIQGHPEFSRAYSSALTNARRDRIPAHRVReALNSLHADVDDLTMARWILNFLQQ 233
Cdd:COG0518   151 VLASSDNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADELAAEELL-AEASLHDPELREAGRRLLRNFLRE 224
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 2-185 3.25e-53

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: 169.73  E-value: 3.25e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485   2 KIGILQCDDVQEalqlefgnyPCMFQNLLNQI-SNDLTWQVYDVRIGEYPEHLDDCDGYISTGSRYGV-NDSLAWLEPLE 79
Cdd:cd01741     1 RILILQHDTPEG---------PGLFEDLLREAgAETIEIDVVDVYAGELLPDLDDYDGLVILGGPMSVdEDDYPWLKKLK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  80 AFVQKAYRAKKPFVGICFGHQLIAKALGGKVDRSEKGWGAGISFNQIVVQTPWMKPQQNG---LDLVVSHQDQVVELPEN 156
Cdd:cd01741    72 ELIRQALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTLTEAGKADPLFAGLpdeFPVFHWHGDTVVELPPG 151

                         170       180
                  ....*....|....*....|....*....
gi 1463651485 157 AQVLAQSSFCLNYMIQIGSSMLGIQGHPE 185
Cdd:cd01741   152 AVLLASSEACPNQAFRYGDRALGLQFHPE 180
PRK09065 PRK09065
glutamine amidotransferase; Provisional
 2-233 3.78e-34

glutamine amidotransferase; Provisional


Pssm-ID: 181635 [Multi-domain]  Cd Length: 237  Bit Score: 122.38  E-value: 3.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485   2 KIGILQCDDVQEALQLEFGNYPCMFQNLLNQISNDLtwQVYDVRIGEYPEHLDDCDGYISTGSRYGVNDSLAWLEPLEAF 81
Cdd:PRK09065    3 PLLIIQTGTPPPSIRARYGDFPHWIRVALGLAEQPV--VVVRVFAGEPLPAPDDFAGVIITGSWAMVTDRLDWSERTADW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  82 VQKAYRAKKPFVGICFGHQLIAKALGGKVDRSEKGWGAG---ISFNQIVVQTPWMK--PQQNGLDLvvSHQDQVVELPEN 156
Cdd:PRK09065   81 LRQAAAAGMPLLGICYGHQLLAHALGGEVGYNPAGRESGtvtVELHPAAADDPLFAglPAQFPAHL--THLQSVLRLPPG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1463651485 157 AQVLAQSSFCLNYMIQIGSSMLGIQGHPEFSRAYSSALTNARRDRIPAHRvREALnSLHADVDDLTMARWIL-NFLQQ 233
Cdd:PRK09065  159 AVVLARSAQDPHQAFRYGPHAWGVQFHPEFTAHIMRAYLRARADCLRREG-LDAR-TLLREVSEAPWARKLLrRFVRL 234
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 55-185 2.88e-19

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: 81.81  E-value: 2.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  55 DCDGYISTGSRYGVNDSLAWLEPLEAFvqkayRAKKPFVGICFGHQLIAKALGGKVDRSEKGwGAGISFNQIVVQTPWMK 134
Cdd:cd01742    41 NPKGIILSGGPSSVYEEDAPRVDPEIF-----ELGVPVLGICYGMQLIAKALGGKVERGDKR-EYGKAEIEIDDSSPLFE 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1463651485 135 PQQNGLDLVVSHQDQVVELPENAQVLAQSSFCLNYMIQIGS-SMLGIQGHPE 185
Cdd:cd01742   115 GLPDEQTVWMSHGDEVVKLPEGFKVIASSDNCPVAAIANEEkKIYGVQFHPE 166
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 83-185 1.14e-17

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 77.74  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  83 QKAYRAKKPFVGICFGHQLIAKALGGKVDRSEKG---------WGAGISFNQI-VVQTPWMkpqqngldlvvSHQDQVVE 152
Cdd:TIGR00888  64 EKIFELGVPVLGICYGMQLMAKQLGGEVGRAEKReygkaeleiLDEDDLFRGLpDESTVWM-----------SHGDKVKE 132

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1463651485 153 LPENAQVLAQSSFCLNYMIQIGSSML-GIQGHPE 185
Cdd:TIGR00888 133 LPEGFKVLATSDNCPVAAMAHEEKPIyGVQFHPE 166
guaA PRK00074
GMP synthase; Reviewed
 86-185 2.96e-15

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 73.93  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  86 YRAKKPFVGICFGHQLIAKALGGKVDRSEKG-WG-------------AGISFNQIVvqtpWMkpqqngldlvvSHQDQVV 151
Cdd:PRK00074   72 FELGVPVLGICYGMQLMAHQLGGKVERAGKReYGraelevdndsplfKGLPEEQDV----WM-----------SHGDKVT 136

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1463651485 152 ELPENAQVLAQSSFCLNYMIQIGS-SMLGIQGHPE 185
Cdd:PRK00074  137 ELPEGFKVIASTENCPIAAIANEErKFYGVQFHPE 171
PRK07053 PRK07053
glutamine amidotransferase; Provisional
 74-185 3.47e-15

glutamine amidotransferase; Provisional


Pssm-ID: 235919 [Multi-domain]  Cd Length: 234  Bit Score: 71.90  E-value: 3.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  74 WLEPLEAFVQKAYRAKKPFVGICFGHQLIAKALGGKV---DRSEKGWGAgISFNQIVVQTPwMKPQQNGLDLVVSHQDQv 150
Cdd:PRK07053   68 FLAPEIALLRQRLAAGLPTLGICLGAQLIARALGARVypgGQKEIGWAP-LTLTDAGRASP-LRHLGAGTPVLHWHGDT- 144

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1463651485 151 VELPENAQVLAQSSFCLNYMIQIGSSMLGIQGHPE 185
Cdd:PRK07053  145 FDLPEGATLLASTPACRHQAFAWGNHVLALQFHPE 179
PRK00758 PRK00758
GMP synthase subunit A; Validated
 91-187 1.05e-14

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 69.50  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  91 PFVGICFGHQLIAKALGGKVDRSEKGWGAGISFNqIVVQTPWMKpqqnGL--DLVV--SHQDQVVELPENAQVLAQSSFC 166
Cdd:PRK00758   69 PILGICLGHQLIAKAFGGEVGRGEYGEYALVEVE-ILDEDDILK----GLppEIRVwaSHADEVKELPDGFEILARSDIC 143

                          90       100
                  ....*....|....*....|..
gi 1463651485 167 -LNYMIQIGSSMLGIQGHPEFS 187
Cdd:PRK00758  144 eVEAMKHKEKPIYGVQFHPEVA 165
PRK06490 PRK06490
glutamine amidotransferase; Provisional
 50-233 2.31e-14

glutamine amidotransferase; Provisional


Pssm-ID: 180590 [Multi-domain]  Cd Length: 239  Bit Score: 69.60  E-value: 2.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  50 PEHLDDCDGYISTGSRYGVNDSLAWLEPLEAFVQKAYRAKKPFVGICFGHQLIAKALGGKVD-----RSEKGW------G 118
Cdd:PRK06490   47 PDTLEDHAGAVIFGGPMSANDPDDFIRREIDWISVPLKENKPFLGICLGAQMLARHLGARVAphpdgRVEIGYyplrptE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485 119 AGISFnqivvqTPWmkPQQngldlvVSH-QDQVVELPENAQVLAQSSFCLNYMIQIGSSMLGIQGHPEFSRAYSSALT-- 195
Cdd:PRK06490  127 AGRAL------MHW--PEM------VYHwHREGFDLPAGAELLATGDDFPNQAFRYGDNAWGLQFHPEVTRAMMHRWVvr 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1463651485 196 NARRDRIPAHRVREAlnslHAD---VDDLTMARWILNFLQQ 233
Cdd:PRK06490  193 GAHRLTLPGAQPRRA----HLEgrlLHDAALRAWLEAFLDH 229
GATase pfam00117
Glutamine amidotransferase class-I;
73-187 2.92e-10

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 57.63  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  73 AWLEPLEAFVQKAYRAKKPFVGICFGHQLIAKALGGKVDRSEK----GWgagisfNQIVVQTPWMKPQQNGLDLVVS--H 146
Cdd:pfam00117  54 GAAGGAIEAIREARELKIPILGICLGHQLLALAFGGKVVKAKKfghhGK------NSPVGDDGCGLFYGLPNVFIVRryH 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1463651485 147 QDQVVE--LPENAQVLAQSSFCLNYM--IQIGSSMLGIQGHPEFS 187
Cdd:pfam00117 128 SYAVDPdtLPDGLEVTATSENDGTIMgiRHKKLPIFGVQFHPESI 172
PLN02347 PLN02347
GMP synthetase
 79-185 2.11e-09

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 57.00  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  79 EAFVQKAYRAKKPFVGICFGHQLIAKALGGKVDRSEKG-WG---------------AGISFNQIVvqtpWMkpqqngldl 142
Cdd:PLN02347   76 EGFFDYCRERGVPVLGICYGMQLIVQKLGGEVKPGEKQeYGrmeirvvcgsqlfgdLPSGETQTV----WM--------- 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1463651485 143 vvSHQDQVVELPENAQVLAQSSFCLNYMIQ-IGSSMLGIQGHPE 185
Cdd:PLN02347  143 --SHGDEAVKLPEGFEVVAKSVQGAVVAIEnRERRIYGLQYHPE 184
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 51-102 2.82e-08

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: 50.67  E-value: 2.82e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1463651485  51 EHLDDCDGYISTGSrYGVNDSLAWLEPLEAFVQKAYRAKKPFVGICFGHQLI 102
Cdd:cd01653    42 VDLDDYDGLILPGG-PGTPDDLARDEALLALLREAAAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 48-102 5.70e-08

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: 49.12  E-value: 5.70e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1463651485  48 EYPEHLDDCDGYISTGSrYGVNDSLAWLEPLEAFVQKAYRAKKPFVGICFGHQLI 102
Cdd:cd03128    39 ESDVDLDDYDGLILPGG-PGTPDDLAWDEALLALLREAAAAGKPVLGICLGAQLL 92
PRK08250 PRK08250
glutamine amidotransferase; Provisional
 80-189 5.92e-08

glutamine amidotransferase; Provisional


Pssm-ID: 181323 [Multi-domain]  Cd Length: 235  Bit Score: 51.51  E-value: 5.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  80 AFVQKAYRAKKPFVGICFGHQLIAKALGGKVDRS-EKGWG--------AGI---SFNQIvvqtpwmkpqqnGLDLVVSH- 146
Cdd:PRK08250   75 RLINQAIKAGKAVIGVCLGAQLIGEALGAKYEHSpEKEIGyfpitlteAGLkdpLLSHF------------GSTLTVGHw 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1463651485 147 QDQVVELPENAQVLAQSSFCLNYMIQIGSSMLGIQGHPEFSRA 189
Cdd:PRK08250  143 HNDMPGLTDQAKVLATSEGCPRQIVQYSNLVYGFQCHMEFTVE 185
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
82-109 1.19e-07

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 51.23  E-value: 1.19e-07
                          10        20
                  ....*....|....*....|....*...
gi 1463651485  82 VQKAYRAKKPFVGICFGHQLIAKALGGK 109
Cdd:PRK12564  241 IRELLEKKIPIFGICLGHQLLALALGAK 268
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 84-115 2.47e-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: 49.07  E-value: 2.47e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1463651485  84 KAYRAKKPFVGICFGHQLIAKALGGKVDRSEK 115
Cdd:cd01743    66 RALAGKVPILGVCLGHQAIAEAFGGKVVRAPE 97
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 82-109 4.94e-07

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 49.63  E-value: 4.94e-07
                          10        20
                  ....*....|....*....|....*...
gi 1463651485  82 VQKAYRAKKPFVGICFGHQLIAKALGGK 109
Cdd:COG0505   240 IRELLGKGIPIFGICLGHQLLALALGAK 267
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 84-115 2.17e-06

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 46.66  E-value: 2.17e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1463651485  84 KAYRAKKPFVGICFGHQLIAKALGGKVDRSEK 115
Cdd:PRK05670   67 REFAGKVPILGVCLGHQAIGEAFGGKVVRAKE 98
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 84-115 3.18e-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: 46.18  E-value: 3.18e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1463651485  84 KAYRAKKPFVGICFGHQLIAKALGGKVDRSEK 115
Cdd:COG0512    66 RAFAGKIPILGVCLGHQAIGEAFGGKVVRAPE 97
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 75-109 3.52e-06

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: 45.95  E-value: 3.52e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1463651485  75 LEPLEAFVQKAYRAKKPFVGICFGHQLIAKALGGK 109
Cdd:cd01744    55 LDEAIKTVRKLLGKKIPIFGICLGHQLLALALGAK 89
CPSaseIIsmall TIGR01368
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ...
 84-109 3.09e-05

carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273580 [Multi-domain]  Cd Length: 357  Bit Score: 44.15  E-value: 3.09e-05
                          10        20
                  ....*....|....*....|....*.
gi 1463651485  84 KAYRAKKPFVGICFGHQLIAKALGGK 109
Cdd:TIGR01368 237 RKLLEKIPIFGICLGHQLLALAFGAK 262
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 53-108 4.18e-05

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: 43.01  E-value: 4.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  53 LDDCDGYISTGSrYGVNDSLAWLEPLE--------------AFVQKAYRAKKPFVGICFGHQLIAKALGG 108
Cdd:pfam07722  56 LDRLDGLLLTGG-PNVDPHFYGEEPSEsggpydpardayelALIRAALARGKPILGICRGFQLLNVALGG 124
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 33-106 6.66e-05

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.


Pssm-ID: 153221 [Multi-domain]  Cd Length: 194  Bit Score: 42.23  E-value: 6.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  33 ISN--DL----TWQVYDVRIGEYPEHLDDCDGYISTGSRyGVNDSLAWLE--PLEAFVQKAYRAKKPFVGICFGHQLIAK 104
Cdd:cd01750     9 ISNftDLdplaREPGVDVRYVEVPEGLGDADLIILPGSK-DTIQDLAWLRkrGLAEAIKNYARAGGPVLGICGGYQMLGK 87


                  ..
gi 1463651485 105 AL 106
Cdd:cd01750    88 YI 89
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 43-187 8.62e-05

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 42.16  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  43 DVRIGEYPEHLDDCDGYISTG-SRYGvnDSLAWLEPLEAFVQKAYRAKKPFVGICFGHQLI---------AKALG---GK 109
Cdd:PRK13143   26 EVVITSDPEEILDADGIVLPGvGAFG--AAMENLSPLRDVILEAARSGKPFLGICLGMQLLfesseegggVRGLGlfpGR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485 110 VDR---SEK----GWgagisfNQIVVQTPwmKPQQNGLD-----LVVSHqdqVVELPENAQVLAQSSFCLNY--MIQIGs 175
Cdd:PRK13143  104 VVRfpaGVKvphmGW------NTVKVVKD--CPLFEGIDgeyvyFVHSY---YAYPDDEDYVVATTDYGIEFpaAVCND- 171

                         170
                  ....*....|..
gi 1463651485 176 SMLGIQGHPEFS 187
Cdd:PRK13143  172 NVFGTQFHPEKS 183
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 50-108 2.06e-04

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: 41.31  E-value: 2.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1463651485  50 PEHLDDCDGYISTGS------RYGVNDSLAWLEP------LE-AFVQKAYRAKKPFVGICFGHQLIAKALGG 108
Cdd:COG2071    44 DELLDRLDGLVLTGGadvdpaLYGEEPHPELGPIdperdaFElALIRAALERGKPVLGICRGMQLLNVALGG 115
PRK07649 PRK07649
aminodeoxychorismate/anthranilate synthase component II;
78-115 2.26e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181066 [Multi-domain]  Cd Length: 195  Bit Score: 40.94  E-value: 2.26e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1463651485  78 LEAFvqKAYRAKKPFVGICFGHQLIAKALGGKVDRSEK 115
Cdd:PRK07649   63 MEVI--RYFAGKIPIFGVCLGHQSIAQVFGGEVVRAER 98
PRK08857 PRK08857
aminodeoxychorismate/anthranilate synthase component II;
69-115 3.69e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181566 [Multi-domain]  Cd Length: 193  Bit Score: 40.25  E-value: 3.69e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1463651485  69 NDSLAWLEPLEAFVqkayrAKKPFVGICFGHQLIAKALGGKVDRSEK 115
Cdd:PRK08857   57 NEAGISLQAIEHFA-----GKLPILGVCLGHQAIAQVFGGQVVRARQ 98
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
80-112 1.01e-03

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 38.88  E-value: 1.01e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1463651485  80 AFVQKAYRAKKPFVGICFGHQLIAKALGGKVDR 112
Cdd:PRK07765   67 DMVRACAAAGTPLLGVCLGHQAIGVAFGATVDR 99
PRK08007 PRK08007
aminodeoxychorismate synthase component 2;
82-115 2.37e-03

aminodeoxychorismate synthase component 2;


Pssm-ID: 181194 [Multi-domain]  Cd Length: 187  Bit Score: 37.59  E-value: 2.37e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1463651485  82 VQKAYRAKKPFVGICFGHQLIAKALGGKVDRSEK 115
Cdd:PRK08007   65 VIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAK 98
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 80-108 2.93e-03

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: 37.56  E-value: 2.93e-03
                          10        20
                  ....*....|....*....|....*....
gi 1463651485  80 AFVQKAYRAKKPFVGICFGHQLIAKALGG 108
Cdd:cd01745    91 ALLRAALERGKPILGICRGMQLLNVALGG 119
hisH PRK13142
imidazole glycerol phosphate synthase subunit HisH; Provisional
 90-196 3.44e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171871 [Multi-domain]  Cd Length: 192  Bit Score: 37.50  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463651485  90 KPFVGICFGHQLIakalggkVDRSEKGWGAGISF---NQIVVQTPWMKPQQNGLDLVVSH----QDQV------VELPEN 156
Cdd:PRK13142   71 KKMIGICLGMQLM-------YEHSDEGDASGLGFipgNISRIQTEYPVPHLGWNNLVSKHpmlnQDVYfvhsyqAPMSEN 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1463651485 157 AQVLAQSSFCLNYMIQIGsSMLGIQGHPEFSRAYSSALTN 196
Cdd:PRK13142  144 VIAYAQYGADIPAIVQFN-NYIGIQFHPEKSGTYGLQILR 182
PLN02771 PLN02771
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
 84-109 3.55e-03

carbamoyl-phosphate synthase (glutamine-hydrolyzing)


Pssm-ID: 178370 [Multi-domain]  Cd Length: 415  Bit Score: 38.04  E-value: 3.55e-03
                          10        20
                  ....*....|....*....|....*.
gi 1463651485  84 KAYRAKKPFVGICFGHQLIAKALGGK 109
Cdd:PLN02771  305 KELLGKVPVFGICMGHQLLGQALGGK 330
trpG_papA TIGR00566
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ...
 78-115 3.59e-03

glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.


Pssm-ID: 273144 [Multi-domain]  Cd Length: 188  Bit Score: 37.08  E-value: 3.59e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1463651485  78 LEAFvqKAYRAKKPFVGICFGHQLIAKALGGKVDRSEK 115
Cdd:TIGR00566  63 LEAI--RHFAGKLPILGVCLGHQAMGQAFGGDVVRANT 98
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
82-113 5.66e-03

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 37.39  E-value: 5.66e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1463651485  82 VQKAYRAKKPFVGICFGHQLIAKALGGKVDRS 113
Cdd:PRK14607   66 VIRHFSGKVPILGVCLGHQAIGYAFGGKIVHA 97
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH