ID   Q5E256_VIBF1            Unreviewed;       430 AA.
AC   Q5E256;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   07-JAN-2015, entry version 81.
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:AAW86890.1};
GN   OrderedLocusNames=VF_2395 {ECO:0000313|EMBL:AAW86890.1};
OS   Vibrio fischeri (strain ATCC 700601 / ES114).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Aliivibrio.
OX   NCBI_TaxID=312309 {ECO:0000313|EMBL:AAW86890.1, ECO:0000313|Proteomes:UP000000537};
RN   [1] {ECO:0000313|EMBL:AAW86890.1, ECO:0000313|Proteomes:UP000000537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114 {ECO:0000313|Proteomes:UP000000537};
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium
RT   with pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00138};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00138};
CC       Note=Binds 1 magnesium or manganese ion per subunit.
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}.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000256|HAMAP-
CC       Rule:MF_00138}.
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DR   EMBL; CP000020; AAW86890.1; -; Genomic_DNA.
DR   RefSeq; WP_011262779.1; NC_006840.2.
DR   RefSeq; YP_205778.1; NC_006840.2.
DR   ProteinModelPortal; Q5E256; -.
DR   SMR; Q5E256; 1-425.
DR   STRING; 312309.VF_2395; -.
DR   EnsemblBacteria; AAW86890; AAW86890; VF_2395.
DR   GeneID; 3279545; -.
DR   KEGG; vfi:VF_2395; -.
DR   PATRIC; 20115542; VBIVibFis127983_2430.
DR   eggNOG; COG0151; -.
DR   HOGENOM; HOG000033463; -.
DR   KO; K01945; -.
DR   OMA; EPKLENV; -.
DR   OrthoDB; EOG69SKD1; -.
DR   BioCyc; AFIS312309:GIWP-2522-MONOMER; -.
DR   Proteomes; UP000000537; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
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; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 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; IPR013816; ATP_grasp_subdomain_2.
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   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|HAMAP-Rule:MF_00138};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000537};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:AAW86890.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000537}.
FT   DOMAIN      109    316       ATP-grasp. {ECO:0000256|HAMAP-Rule:
FT                                MF_00138}.
FT   NP_BIND     135    196       ATP. {ECO:0000256|HAMAP-Rule:MF_00138}.
FT   METAL       286    286       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_00138}.
FT   METAL       288    288       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_00138}.
SQ   SEQUENCE   430 AA;  45730 MW;  1AE178734F1D0D67 CRC64;
     MNVLIIGAGG REHALGWKAA QNPNVETVFI APGNAGTALE PKLENVAIDV EDIAALVAFA
     KEKAIELTIV GPEAPLVIGV VDAFREADLP IFGPTKAAAQ LEGSKAFTKD FLARHDIPTG
     SYANFTEIEP ALAYVREQGA PIVVKADGLA AGKGVIVAMT LEEAEDAIKD MLAGNAFGEA
     GSRVVIEEFL EGEEASFIVM VDGASVLPMA TSQDHKRVGD KDTGPNTGGM GAYSPAPVVT
     PEIHNRILEE VIYPTVRGMD AEGAPYTGFL YAGLMIDTEG TPKVIEYNCR FGDPETQPIM
     MRMESDLVEL CLMAIDEKLD EAESKWDPRA SIGVVLAAGG YPADYAKGDV ISLPSEETEG
     QKIFHAGTTN NDAGDVVTNG GRVLCATALG NTVSEAQERA YELAKQVSWN GMFHRNDIGY
     RAIARELETK
//