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Database: UniProt
Entry: H5V7K2_ATLHE
LinkDB: H5V7K2_ATLHE
Original site: H5V7K2_ATLHE 
ID   H5V7K2_ATLHE            Unreviewed;       430 AA.
AC   H5V7K2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   05-JUN-2019, entry version 40.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000256|HAMAP-Rule:MF_00138,
GN   ECO:0000313|EMBL:GAB53960.1};
GN   ORFNames=EH105704_25_00020 {ECO:0000313|EMBL:GAB53960.1};
OS   Atlantibacter hermannii NBRC 105704.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Atlantibacter.
OX   NCBI_TaxID=1115512 {ECO:0000313|EMBL:GAB53960.1, ECO:0000313|Proteomes:UP000010297};
RN   [1] {ECO:0000313|EMBL:GAB53960.1, ECO:0000313|Proteomes:UP000010297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 105704 {ECO:0000313|EMBL:GAB53960.1,
RC   ECO:0000313|Proteomes:UP000010297};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Escherichia hermannii NBRC 105704.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58089,
CC         ChEBI:CHEBI:58457, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00138};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-diphosphate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00138}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:GAB53960.1}.
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DR   EMBL; BAFF01000025; GAB53960.1; -; Genomic_DNA.
DR   RefSeq; WP_002438602.1; NZ_BAFF01000025.1.
DR   STRING; 1115512.EH105704_25_00020; -.
DR   EnsemblBacteria; GAB53960; GAB53960; EH105704_25_00020.
DR   OrthoDB; 932854at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000010297; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.90.600.10; -; 1.
DR   HAMAP; MF_00138; GARS; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   InterPro; IPR000115; PRibGlycinamide_synth.
DR   InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR   InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR   InterPro; IPR020559; PRibGlycinamide_synth_CS.
DR   InterPro; IPR020562; PRibGlycinamide_synth_N.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF01071; GARS_A; 1.
DR   Pfam; PF02843; GARS_C; 1.
DR   Pfam; PF02844; GARS_N; 1.
DR   SMART; SM01210; GARS_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR00877; purD; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00184; GARS; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010297};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:GAB53960.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010297}.
FT   DOMAIN      109    316       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION      210    234       Disordered. {ECO:0000256|MobiDB-lite:
FT                                H5V7K2}.
SQ   SEQUENCE   430 AA;  45979 MW;  5E86E1EF02406198 CRC64;
     MKVLVIGNGG REHALAWKAA QSPRVSTVFV APGNAGTALE PTLQNVAINA TDIDGLLHFA
     QNEKIDLTIV GPEAPLVIGV VDAFRAAGLK IFGPTQGAAQ LEGSKAFTKD FLARHNIPTA
     EYQNFTEVEP ALAYIREKGA PIVIKADGLA AGKGVIVAMT LEEAESAARD MLAGNAFGDA
     GHRIVVEEFL DGEEASFIVM VDGEHVEPMA TSQDHKRVGD GDTGPNTGGM GAYSPAPVVT
     ADVHQRTMER IIWPTVRGMA AEGNTYTGFL YAGLMIDKQG NPKVIEFNCR FGDPETQPIM
     LRLQSDLVEL CLAACEGKLN DVKSRWDTRP SLGVVMAAGG YPADYRTGDE IHGLPLADVV
     DGKVFHAGTK LADDDRVLTN GGRVLCVTAL GDTVAQAQQR AYALMKDIHW DGSFCRHDIG
     YRAIERENAK
//
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