(data stored in SCRATCH zone)

SWISSPROT: Q3IIC5_PSEHT

ID   Q3IIC5_PSEHT            Unreviewed;       429 AA.
AC   Q3IIC5;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 99.
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:CAI85441.1};
GN   OrderedLocusNames=PSHAa0343 {ECO:0000313|EMBL:CAI85441.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85441.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85441.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP
CC       + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.
CC       {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}.
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DR   EMBL; CR954246; CAI85441.1; -; Genomic_DNA.
DR   RefSeq; WP_011327055.1; NC_007481.1.
DR   ProteinModelPortal; Q3IIC5; -.
DR   STRING; 326442.PSHAa0343; -.
DR   EnsemblBacteria; CAI85441; CAI85441; PSHAa0343.
DR   KEGG; pha:PSHAa0343; -.
DR   PATRIC; fig|326442.8.peg.326; -.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033463; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   OrthoDB; POG091H02DZ; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000006843; Chromosome I.
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-HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP.
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.
DR   InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR   InterPro; IPR000115; PRibGlycinamide_synth.
DR   InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
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;
DR   PRODOM; Q3IIC5.
DR   SWISS-2DPAGE; Q3IIC5.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:CAI85441.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843}.
FT   DOMAIN      109    316       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   429 AA;  45824 MW;  96EAEEA79D2C6DA6 CRC64;
     MNVLVIGSGG REHALAFKAA QNTKVNTVFV APGNAGTALE PKLENVAINV DDLDGLLQFA
     QQNNVELTIV GPEIPLVLGV VDKFREHGLA IFGPTAGAAQ LEGSKSFTKD FLARHNIPSG
     DYQTFEQVAP ALAYLKEKGA PIVIKADGLA AGKGVIVAMT EAEAEDAIRD MLAGNAFGDA
     GSRVVIEEFL EGEEASFIVM VDGKNVLPFA TSQDHKRAYN GDAGPNTGGM GAYSPAPVVT
     DEIHQRIMNE VIYPTVEGMA SEGHPYTGFL YAGLMIDTDG TPKVIEYNCR FGDPETQPMM
     LRLQSDLVEL IEAANRVELD KTTIEFDPRA AVGVVLAAKG YPGDYPKGDV ISGLQVDYPA
     GEKVFHAGTK QNGNDVVTAG GRVLCATALG NTVTEAQQRA YELIKQLSWD GMEYRTDIAY
     RAIAREQNS
//

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