ID D9QCB4_CORP2 Unreviewed; 422 AA.
AC D9QCB4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|ARBA:ARBA00013255, ECO:0000256|HAMAP-Rule:MF_00138};
DE EC=6.3.4.13 {ECO:0000256|ARBA:ARBA00013255, ECO:0000256|HAMAP-Rule:MF_00138};
DE AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138};
DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|ARBA:ARBA00042242, ECO:0000256|HAMAP-Rule:MF_00138};
DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|ARBA:ARBA00042864, ECO:0000256|HAMAP-Rule:MF_00138};
GN Name=purD {ECO:0000256|HAMAP-Rule:MF_00138,
GN ECO:0000313|EMBL:ADL11190.1};
GN ORFNames=CPC231_08800 {ECO:0000313|EMBL:ADL11190.1};
OS Corynebacterium pseudotuberculosis (strain C231).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL11190.1, ECO:0000313|Proteomes:UP000000276};
RN [1] {ECO:0000313|EMBL:ADL11190.1, ECO:0000313|Proteomes:UP000000276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C231 {ECO:0000313|EMBL:ADL11190.1,
RC ECO:0000313|Proteomes:UP000000276};
RX PubMed=21037006; DOI=.1128/JB.01211-10;
RG Consortium: Rede Paraense de Genomica e Proteomica (RPGP);
RA Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T.,
RA Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S.,
RA Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F.,
RA de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.;
RT "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a
RT strain isolated from a cow in Israel with bovine mastitis.";
RL J. Bacteriol. 193:323-324(2011).
RN [2] {ECO:0000313|EMBL:ADL11190.1, ECO:0000313|Proteomes:UP000000276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C231 {ECO:0000313|EMBL:ADL11190.1,
RC ECO:0000313|Proteomes:UP000000276};
RX PubMed=21533164; DOI=10.1371/journal.pone.0018551;
RA Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R.,
RA Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., Turk M.Z.,
RA Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., Castro T.L.,
RA Abreu V.A., Trost E., Baumbach J., Tauch A., Schneider M.P., McCulloch J.,
RA Cerdeira L.T., Ramos R.T., Zerlotini A., Dominitini A., Resende D.M.,
RA Coser E.M., Oliveira L.M., Pedrosa A.L., Vieira C.U., Guimaraes C.T.,
RA Bartholomeu D.C., Oliveira D.M., Santos F.R., Rabelo E.M., Lobo F.P.,
RA Franco G.R., Costa A.F., Castro I.M., Dias S.R., Ferro J.A., Ortega J.M.,
RA Paiva L.V., Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P.,
RA Falcao P.R., Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C.,
RA Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.;
RT "Evidence for reductive genome evolution and lateral acquisition of
RT virulence functions in two Corynebacterium pseudotuberculosis strains.";
RL PLoS ONE 6:E18551-E18551(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate;
CC Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681,
CC ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00138};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 2/2. {ECO:0000256|ARBA:ARBA00005174,
CC ECO:0000256|HAMAP-Rule:MF_00138}.
CC -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|ARBA:ARBA00038345,
CC ECO:0000256|HAMAP-Rule:MF_00138}.
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DR EMBL; CP001829; ADL11190.1; -; Genomic_DNA.
DR RefSeq; WP_014401366.1; NC_017301.2.
DR AlphaFoldDB; D9QCB4; -.
DR STRING; 681645.CpC231_1730; -.
DR KEGG; cpq:CPC231_08800; -.
DR PATRIC; fig|681645.3.peg.1810; -.
DR eggNOG; COG0151; Bacteria.
DR HOGENOM; CLU_027420_3_1_11; -.
DR OrthoDB; 9807240at2; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000000276; Chromosome.
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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.90.600.10; Phosphoribosylglycinamide synthetase, C-terminal domain; 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 NCBIfam; TIGR00877; purD; 1.
DR PANTHER; PTHR43472; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE; 1.
DR PANTHER; PTHR43472:SF1; PHOSPHORIBOSYLAMINE--GLYCINE LIGASE, CHLOROPLASTIC; 1.
DR Pfam; PF01071; GARS_A; 1.
DR Pfam; PF02843; GARS_C; 1.
DR Pfam; PF02844; GARS_N; 1.
DR SMART; SM01209; GARS_A; 1.
DR SMART; SM01210; GARS_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00184; GARS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00138};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00138}; Reference proteome {ECO:0000313|Proteomes:UP000000276}.
FT DOMAIN 109..312
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 422 AA; 43772 MW; DA9D69033B964113 CRC64;
MHILVIGSGA REHALALGLS KDPAVTEIHV APGNVGMESI ATVHAEATQV DDPDAMLKIA
QETHADLVVV GPEIPLVAGV ADTLRSHGFA VFGPNKDAAQ IEGSKAFAKD VMAKAGVKTA
RAEQIVPGAS DAEREAALDN FGPHYVVKDD GLAGGKGVVV TKDRAQARAH VDAVLAAGNP
VLLESFLDGP EVSLFCLVDG ETVVPLLPAQ DHKRAHDNDE GPNTGGMGAY TPLPWLPEDG
VQRIVDEVCV PVAREMVARG CAYSGLLYAG IAWGEDGPAV VEFNCRFGDP ETQAVLALLK
TPLAGALHAV ATEKLAELPP LEWEDGYALT VVLAAEGYPQ NPRKGGEIVG AEDPAVLHAG
TARDADGKLV AAGGRVLNVI GTGASLIEAR DKAYSVLNNI TLAGSHYRSD IALPAVEGKI
TI
//
