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Conserved domains on  [gi|1371546796|ref|XP_024329120|]
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pyridoxine biosynthesis protein PDX2 [Plasmodium falciparum 3D7]

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

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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 ...
 6-172 2.06e-64

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 cd01749:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 183  Bit Score: 195.82  E-value: 2.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   6 IGVLSLQGDFEPHInhfIKLQIPSLNIIQVRNVHDLGLCDGLVIPGGESTTVRRCCAYENdtLYNALVHFIHVlKKPIWG 85
Cdd:cd01749     1 IGVLALQGDFREHI---RALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTG--LLDPLREFIRA-GKPVFG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  86 TCAGCILLSKNVENIklysnfGNKFSFGGLDITICRNFYGSQV----------------------------KVLATFSHE 137
Cdd:cd01749    75 TCAGLILLAKEVEDQ------GGQPLLGLLDITVRRNAFGRQVdsfeadldipglglgpfpavfirapvieEVGPGVEVL 148

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1371546796 138 SYGPNIIAAVEQNNCLGTVFHPELLPHTAFQQYFY 172
Cdd:cd01749   149 AEYDGKIVAVRQGNVLATSFHPELTDDTRIHEYFL 183
 
Name Accession Description Interval E-value
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 6-172 2.06e-64

Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6.


Pssm-ID: 153220 [Multi-domain]  Cd Length: 183  Bit Score: 195.82  E-value: 2.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   6 IGVLSLQGDFEPHInhfIKLQIPSLNIIQVRNVHDLGLCDGLVIPGGESTTVRRCCAYENdtLYNALVHFIHVlKKPIWG 85
Cdd:cd01749     1 IGVLALQGDFREHI---RALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTG--LLDPLREFIRA-GKPVFG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  86 TCAGCILLSKNVENIklysnfGNKFSFGGLDITICRNFYGSQV----------------------------KVLATFSHE 137
Cdd:cd01749    75 TCAGLILLAKEVEDQ------GGQPLLGLLDITVRRNAFGRQVdsfeadldipglglgpfpavfirapvieEVGPGVEVL 148

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1371546796 138 SYGPNIIAAVEQNNCLGTVFHPELLPHTAFQQYFY 172
Cdd:cd01749   149 AEYDGKIVAVRQGNVLATSFHPELTDDTRIHEYFL 183
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
 5-179 2.09e-49

Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440080 [Multi-domain]  Cd Length: 191  Bit Score: 157.92  E-value: 2.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   5 TIGVLSLQGDFEPHINHFIKLQIpslNIIQVRNVHDLGLCDGLVIPGGESTTVRRCCAYENdtLYNALVHFIHVlKKPIW 84
Cdd:COG0311     2 KIGVLALQGDVREHIRALERLGA---EVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFG--LLEPLRERIAA-GLPVF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  85 GTCAGCILLSKNVENiklysnfGNKFSFGGLDITICRNFYGSQ----------------------------------VKV 130
Cdd:COG0311    76 GTCAGLILLAKEIED-------PDQPTLGLLDITVRRNAFGRQvdsfeadldipglgdgpfpavfirapyieevgpgVEV 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1371546796 131 LATFshesygPNIIAAVEQNNCLGTVFHPELLPHTAFQQYFYEKVKNYK 179
Cdd:COG0311   149 LATV------DGRIVAVRQGNILATSFHPELTDDLRVHEYFLEMVRGAK 191
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
5-176 8.20e-46

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 148.77  E-value: 8.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   5 TIGVLSLQGDFEPHINHFIKLQIPSlniIQVRNVHDLGLCDGLVIPGGESTTVRRcCAYENDtLYNALVHFIHVlKKPIW 84
Cdd:PRK13525    3 KIGVLALQGAVREHLAALEALGAEA---VEVRRPEDLDEIDGLILPGGESTTMGK-LLRDFG-LLEPLREFIAS-GLPVF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  85 GTCAGCILLSKNVENiklysnfGNKFSFGGLDITICRNFYGSQV--------------KVLATFSH----ESYGPNI--- 143
Cdd:PRK13525   77 GTCAGMILLAKEIEG-------YEQEHLGLLDITVRRNAFGRQVdsfeaeldikglgePFPAVFIRapyiEEVGPGVevl 149

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1371546796 144 ------IAAVEQNNCLGTVFHPELLPHTAFQQYFYEKVK 176
Cdd:PRK13525  150 atvggrIVAVRQGNILATSFHPELTDDTRVHRYFLEMVK 188
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
 6-173 1.22e-30

pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is synthesized by the PdxA/PdxJ pathway in some species (mostly within the gamma subdivision of the proteobacteria) and by the Pdx1/Pdx2 pathway in most other organisms. This family describes Pdx2, the glutaminase subunit of the PLP synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 274792 [Multi-domain]  Cd Length: 184  Bit Score: 109.83  E-value: 1.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   6 IGVLSLQGDFEPHINHFIKLQIPSlniIQVRNVHDLGLCDGLVIPGGESTTVRRCCAYEN--DTLYNALVHfihvlKKPI 83
Cdd:TIGR03800   2 IGVLALQGAVREHARALEALGVEG---VEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGmfEPLRNFILS-----GLPV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  84 WGTCAGCILLSKNVeniklysnFGNKFSF-GGLDITICRNFYGSQ----------------------------------V 128
Cdd:TIGR03800  74 FGTCAGLIMLAKEI--------IGQKEGQlGLLDMTVERNAYGRQvdsfeaevdikgvgddpitgvfirapkivsvgngV 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1371546796 129 KVLATFShesygpNIIAAVEQNNCLGTVFHPELLPHTAFQQYFYE 173
Cdd:TIGR03800 146 EILAKVG------NRIVAVRQGNILVSSFHPELTDDHRVHEYFLE 184
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
 8-175 1.85e-30

SNO glutamine amidotransferase family; This family and its amidotransferase domain was first described in. It is predicted that members of this family are involved in the pyridoxine biosynthetic pathway, based on the proximity and co-regulation of the corresponding genes and physical interaction between the members of pfam01174 and pfam01680.


Pssm-ID: 334414 [Multi-domain]  Cd Length: 188  Bit Score: 109.54  E-value: 1.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   8 VLSLQGDFEPHINHFIKLQIPSLniiQVRNVHDLGLCDGLVIPGGESTTVRRCCayENDTLYNALVHFIHVLKKPIWGTC 87
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAENK---TVKRPEDLAQCDALIIPGGESTAMSLLA--KRYGFYEPLYEFVHNPNKPIWGTC 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  88 AGCILLSKNVENIKLysnfgnkFSFGGLDITICRNFYGSQV--------------KVLATF------------SHE---S 138
Cdd:pfam01174  76 AGLILLSKQLGNELV-------KTLGLLKVTVKRNAFGRQVdsfekecdfknlipKFPGVFirapvieeildpEVVvvlY 148

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1371546796 139 YGPNIIAAVEQNNCLGTVFHPELLPH-TAFQQYFYEKV 175
Cdd:pfam01174 149 ELDGKIVVAKQGNILATSFHPELAEDdYRVHDWFVENF 186
 
Name Accession Description Interval E-value
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 6-172 2.06e-64

Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6.


Pssm-ID: 153220 [Multi-domain]  Cd Length: 183  Bit Score: 195.82  E-value: 2.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   6 IGVLSLQGDFEPHInhfIKLQIPSLNIIQVRNVHDLGLCDGLVIPGGESTTVRRCCAYENdtLYNALVHFIHVlKKPIWG 85
Cdd:cd01749     1 IGVLALQGDFREHI---RALERLGVEVIEVRTPEDLEGIDGLIIPGGESTTIGKLLRRTG--LLDPLREFIRA-GKPVFG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  86 TCAGCILLSKNVENIklysnfGNKFSFGGLDITICRNFYGSQV----------------------------KVLATFSHE 137
Cdd:cd01749    75 TCAGLILLAKEVEDQ------GGQPLLGLLDITVRRNAFGRQVdsfeadldipglglgpfpavfirapvieEVGPGVEVL 148

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1371546796 138 SYGPNIIAAVEQNNCLGTVFHPELLPHTAFQQYFY 172
Cdd:cd01749   149 AEYDGKIVAVRQGNVLATSFHPELTDDTRIHEYFL 183
PdxT COG0311
Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport ...
 5-179 2.09e-49

Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) [Coenzyme transport and metabolism]; Pyridoxal 5'-phosphate synthase subunit PdxT (glutamine amidotransferase) is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440080 [Multi-domain]  Cd Length: 191  Bit Score: 157.92  E-value: 2.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   5 TIGVLSLQGDFEPHINHFIKLQIpslNIIQVRNVHDLGLCDGLVIPGGESTTVRRCCAYENdtLYNALVHFIHVlKKPIW 84
Cdd:COG0311     2 KIGVLALQGDVREHIRALERLGA---EVVEVRRPEDLEGLDGLIIPGGESTTIGKLLRRFG--LLEPLRERIAA-GLPVF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  85 GTCAGCILLSKNVENiklysnfGNKFSFGGLDITICRNFYGSQ----------------------------------VKV 130
Cdd:COG0311    76 GTCAGLILLAKEIED-------PDQPTLGLLDITVRRNAFGRQvdsfeadldipglgdgpfpavfirapyieevgpgVEV 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1371546796 131 LATFshesygPNIIAAVEQNNCLGTVFHPELLPHTAFQQYFYEKVKNYK 179
Cdd:COG0311   149 LATV------DGRIVAVRQGNILATSFHPELTDDLRVHEYFLEMVRGAK 191
PRK13525 PRK13525
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;
5-176 8.20e-46

pyridoxal 5'-phosphate synthase glutaminase subunit PdxT;


Pssm-ID: 237411 [Multi-domain]  Cd Length: 189  Bit Score: 148.77  E-value: 8.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   5 TIGVLSLQGDFEPHINHFIKLQIPSlniIQVRNVHDLGLCDGLVIPGGESTTVRRcCAYENDtLYNALVHFIHVlKKPIW 84
Cdd:PRK13525    3 KIGVLALQGAVREHLAALEALGAEA---VEVRRPEDLDEIDGLILPGGESTTMGK-LLRDFG-LLEPLREFIAS-GLPVF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  85 GTCAGCILLSKNVENiklysnfGNKFSFGGLDITICRNFYGSQV--------------KVLATFSH----ESYGPNI--- 143
Cdd:PRK13525   77 GTCAGMILLAKEIEG-------YEQEHLGLLDITVRRNAFGRQVdsfeaeldikglgePFPAVFIRapyiEEVGPGVevl 149

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1371546796 144 ------IAAVEQNNCLGTVFHPELLPHTAFQQYFYEKVK 176
Cdd:PRK13525  150 atvggrIVAVRQGNILATSFHPELTDDTRVHRYFLEMVK 188
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 4-177 1.62e-40

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 135.78  E-value: 1.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   4 ITIGVLSLQGDFEPHINHF---IKLQIPSLNIIQVRNVHDLGLCDGLVIPGGESTTVRRCCAYENdtLYNALVHFIHvLK 80
Cdd:PRK13527    1 MKIGVLALQGDVEEHIDALkraLDELGIDGEVVEVRRPGDLPDCDALIIPGGESTTIGRLMKREG--ILDEIKEKIE-EG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  81 KPIWGTCAGCILLSKNVENIKLySNFGNKFsFGGLDITICRNFYGSQ--------------------------------- 127
Cdd:PRK13527   78 LPILGTCAGLILLAKEVGDDRV-TKTEQPL-LGLMDVTVKRNAFGRQrdsfeaeidlsgldgpfhavfirapaitkvggd 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1371546796 128 VKVLATFshesygPNIIAAVEQNNCLGTVFHPELLPHTAFQQYFYEKVKN 177
Cdd:PRK13527  156 VEVLAKL------DDRIVAVEQGNVLATAFHPELTDDTRIHEYFLKKVKG 199
PLN02832 PLN02832
glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex
 4-179 5.74e-37

glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase complex


Pssm-ID: 215446 [Multi-domain]  Cd Length: 248  Bit Score: 127.90  E-value: 5.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   4 ITIGVLSLQGDFEPHINHFIKLQIPSlniIQVRNVHDLGLCDGLVIPGGESTTVRRCCAYENdtLYNALVHFIHvLKKPI 83
Cdd:PLN02832    2 MAIGVLALQGSFNEHIAALRRLGVEA---VEVRKPEQLEGVSGLIIPGGESTTMAKLAERHN--LFPALREFVK-SGKPV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  84 WGTCAGCILLSKNVENIKLysnfGNKFSFGGLDITICRNFYGSQ------------------------------------ 127
Cdd:PLN02832   76 WGTCAGLIFLAERAVGQKE----GGQELLGGLDCTVHRNFFGSQinsfetelpvpelaaseggpetfravfirapailsv 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1371546796 128 ---VKVLA-----------TFSHESYGPN-IIAAVEQNNCLGTVFHPELLPHTAFQQYFYEKVKNYK 179
Cdd:PLN02832  152 gpgVEVLAeyplpsekalySSSTDAEGRDkVIVAVKQGNLLATAFHPELTADTRWHSYFVKMVSESE 218
PLP_synth_Pdx2 TIGR03800
pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is ...
 6-173 1.22e-30

pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Pyridoxal 5'-phosphate (PLP) is synthesized by the PdxA/PdxJ pathway in some species (mostly within the gamma subdivision of the proteobacteria) and by the Pdx1/Pdx2 pathway in most other organisms. This family describes Pdx2, the glutaminase subunit of the PLP synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 274792 [Multi-domain]  Cd Length: 184  Bit Score: 109.83  E-value: 1.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   6 IGVLSLQGDFEPHINHFIKLQIPSlniIQVRNVHDLGLCDGLVIPGGESTTVRRCCAYEN--DTLYNALVHfihvlKKPI 83
Cdd:TIGR03800   2 IGVLALQGAVREHARALEALGVEG---VEVKRPEQLDEIDGLIIPGGESTTISRLLDKYGmfEPLRNFILS-----GLPV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  84 WGTCAGCILLSKNVeniklysnFGNKFSF-GGLDITICRNFYGSQ----------------------------------V 128
Cdd:TIGR03800  74 FGTCAGLIMLAKEI--------IGQKEGQlGLLDMTVERNAYGRQvdsfeaevdikgvgddpitgvfirapkivsvgngV 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1371546796 129 KVLATFShesygpNIIAAVEQNNCLGTVFHPELLPHTAFQQYFYE 173
Cdd:TIGR03800 146 EILAKVG------NRIVAVRQGNILVSSFHPELTDDHRVHEYFLE 184
SNO pfam01174
SNO glutamine amidotransferase family; This family and its amidotransferase domain was first ...
 8-175 1.85e-30

SNO glutamine amidotransferase family; This family and its amidotransferase domain was first described in. It is predicted that members of this family are involved in the pyridoxine biosynthetic pathway, based on the proximity and co-regulation of the corresponding genes and physical interaction between the members of pfam01174 and pfam01680.


Pssm-ID: 334414 [Multi-domain]  Cd Length: 188  Bit Score: 109.54  E-value: 1.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   8 VLSLQGDFEPHINHFIKLQIPSLniiQVRNVHDLGLCDGLVIPGGESTTVRRCCayENDTLYNALVHFIHVLKKPIWGTC 87
Cdd:pfam01174   1 VLALQGAVEEHEEAIKKCGAENK---TVKRPEDLAQCDALIIPGGESTAMSLLA--KRYGFYEPLYEFVHNPNKPIWGTC 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  88 AGCILLSKNVENIKLysnfgnkFSFGGLDITICRNFYGSQV--------------KVLATF------------SHE---S 138
Cdd:pfam01174  76 AGLILLSKQLGNELV-------KTLGLLKVTVKRNAFGRQVdsfekecdfknlipKFPGVFirapvieeildpEVVvvlY 148

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1371546796 139 YGPNIIAAVEQNNCLGTVFHPELLPH-TAFQQYFYEKV 175
Cdd:pfam01174 149 ELDGKIVVAKQGNILATSFHPELAEDdYRVHDWFVENF 186
PRK13526 PRK13526
glutamine amidotransferase subunit PdxT; Provisional
 4-171 5.26e-17

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 184113 [Multi-domain]  Cd Length: 179  Bit Score: 74.60  E-value: 5.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   4 ITIGVLSLQGDFEPHINHFIKLQIpslNIIQVRNVHDLGLCDGLVIPGGESTTVRRCcaYENDTLYNALVHFIHvlKKPI 83
Cdd:PRK13526    3 QKVGVLAIQGGYQKHADMFKSLGV---EVKLVKFNNDFDSIDRLVIPGGESTTLLNL--LNKHQIFDKLYNFCS--SKPV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  84 WGTCAGCILLSKNVENIKLysnfgnkfsfggLDITICRNFYGSQVKVLAT---FSHESYGPNIIAA-------------- 146
Cdd:PRK13526   76 FGTCAGSIILSKGEGYLNL------------LDLEVQRNAYGRQVDSFVAdisFNDKNITGVFIRApkfivvgnqvdils 143

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1371546796 147 --------VEQNNCLGTVFHPELLPHTAFQQYF 171
Cdd:PRK13526  144 kyqnspvlLRQANILVSSFHPELTQDPTVHEYF 176
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 6-93 1.43e-06

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: 44.50  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   6 IGVLSLQGDFEPHINHF--------IKLQIPSLNIIQVRNVHDLGLCDGLVIPGGESTTVRRccaYENDTLYNALVHFiH 77
Cdd:cd03128     1 VAVLLFGGSEELELASPldalreagAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDL---AWDEALLALLREA-A 76

                          90
                  ....*....|....*.
gi 1371546796  78 VLKKPIWGTCAGCILL 93
Cdd:cd03128    77 AAGKPVLGICLGAQLL 92
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 6-93 1.88e-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: 44.90  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796   6 IGVLSLQGDFEPHINHF--------IKLQIPSLNIIQVRNVHDLGLCDGLVIPGGESTTVRRccaYENDTLYNALVHFIH 77
Cdd:cd01653     1 VAVLLFPGFEELELASPldalreagAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDL---ARDEALLALLREAAA 77

                          90
                  ....*....|....*.
gi 1371546796  78 vLKKPIWGTCAGCILL 93
Cdd:cd01653    78 -AGKPILGICLGAQLL 92
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 139-160 2.61e-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: 36.94  E-value: 2.61e-03
                          10        20
                  ....*....|....*....|..
gi 1371546796 139 YGPNIIAAVEQNNCLGTVFHPE 160
Cdd:COG0118   164 YGVPFTAAVERGNVFGTQFHPE 185
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 35-160 3.79e-03

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 36.53  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  35 VRNVHDLGLCDGLVIPGGES-----TTVRRccaYENDTLYNALVhfihVLKKPIWGTCAGC-ILLSK------------- 95
Cdd:TIGR01855  28 VKDSKEAELADKLILPGVGAfgaamARLRE---NGLDLFVELVV----RLGKPVLGICLGMqLLFERseegggvpglgli 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371546796  96 --NVENIK-----------LYSNFGNKFsFGGLDITICRNF---YGSQVKVLATFSHESYGPNIIAAVEQNNCLGTVFHP 159
Cdd:TIGR01855 101 kgNVVKLEarkvphmgwneVHPVKESPL-LNGIDEGAYFYFvhsYYAVCEEEAVLAYADYGEKFPAAVQKGNIFGTQFHP 179


                  .
gi 1371546796 160 E 160
Cdd:TIGR01855 180 E 180
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 139-160 7.32e-03

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: 35.55  E-value: 7.32e-03
                          10        20
                  ....*....|....*....|..
gi 1371546796 139 YGPNIIAAVEQNNCLGTVFHPE 160
Cdd:cd01748   163 YGGKFPAAVEKDNIFGTQFHPE 184
 
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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