ID A0A0T7RZR4_SALET Unreviewed; 429 AA.
AC A0A0T7RZR4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:SUE49318.1};
GN ORFNames=B7N00_22555 {ECO:0000313|EMBL:EDG5019724.1}, B7N01_22550
GN {ECO:0000313|EMBL:EDG4997183.1}, B7N35_22040
GN {ECO:0000313|EMBL:EDG5128692.1}, B7N72_21145
GN {ECO:0000313|EMBL:EDG5372600.1}, B7N78_22215
GN {ECO:0000313|EMBL:EDG5282468.1}, B7N80_22380
GN {ECO:0000313|EMBL:EDG5291104.1}, B7N84_22170
GN {ECO:0000313|EMBL:EDG5269037.1}, DRU31_22780
GN {ECO:0000313|EMBL:EBS2455093.1}, E0916_23135
GN {ECO:0000313|EMBL:ECF1448820.1}, EJV93_22990
GN {ECO:0000313|EMBL:ECA2724039.1}, ERS008202_04031
GN {ECO:0000313|EMBL:CNU99350.1}, EWC73_22305
GN {ECO:0000313|EMBL:ECE8538902.1}, G0B02_23850
GN {ECO:0000313|EMBL:HAC6382089.1}, G0D18_23285
GN {ECO:0000313|EMBL:HAC6683519.1}, G2206_22580
GN {ECO:0000313|EMBL:HAE0437519.1}, NCTC5754_04322
GN {ECO:0000313|EMBL:SUE49318.1};
OS Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=58097 {ECO:0000313|EMBL:SUE49318.1, ECO:0000313|Proteomes:UP000254190};
RN [1] {ECO:0000313|EMBL:CNU99350.1, ECO:0000313|Proteomes:UP000039541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3476 {ECO:0000313|EMBL:CNU99350.1,
RC ECO:0000313|Proteomes:UP000039541};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HAC6382089.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6382089.1}, M123
RC {ECO:0000313|EMBL:HAC6683519.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0437519.1};
RX PubMed=30286803;
RA Souvorov A., Agarwala R., Lipman D.J.;
RT "SKESA: strategic k-mer extension for scrupulous assemblies.";
RL Genome Biol. 19:153-153(2018).
RN [3] {ECO:0000313|EMBL:SUE49318.1, ECO:0000313|Proteomes:UP000254190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5754 {ECO:0000313|EMBL:SUE49318.1,
RC ECO:0000313|Proteomes:UP000254190};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:HAC6683519.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCW_3301 {ECO:0000313|EMBL:HAC6382089.1}, M123
RC {ECO:0000313|EMBL:HAC6683519.1}, and MS140073
RC {ECO:0000313|EMBL:HAE0437519.1};
RG NCBI Pathogen Detection Project;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:ECE8538902.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=136768 {ECO:0000313|EMBL:EDG4997183.1}, 138330
RC {ECO:0000313|EMBL:EDG5291104.1}, 143652
RC {ECO:0000313|EMBL:EDG5372600.1}, 273631
RC {ECO:0000313|EMBL:EDG5019724.1}, 330535
RC {ECO:0000313|EMBL:EDG5269037.1}, 333944
RC {ECO:0000313|EMBL:EDG5282468.1}, 337042
RC {ECO:0000313|EMBL:EDG5128692.1}, 387147
RC {ECO:0000313|EMBL:EBS2455093.1}, 470200
RC {ECO:0000313|EMBL:ECE8538902.1}, 598023
RC {ECO:0000313|EMBL:ECA2724039.1}, and 692616
RC {ECO:0000313|EMBL:ECF1448820.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Monomer. {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; CQPC01000073; CNU99350.1; -; Genomic_DNA.
DR EMBL; AAGUWJ010000030; EBS2455093.1; -; Genomic_DNA.
DR EMBL; AAHTVM010000023; ECA2724039.1; -; Genomic_DNA.
DR EMBL; AAIJHK010000031; ECE8538902.1; -; Genomic_DNA.
DR EMBL; AAIKGE010000027; ECF1448820.1; -; Genomic_DNA.
DR EMBL; AAMEJW010000037; EDG4997183.1; -; Genomic_DNA.
DR EMBL; AAMEJY010000026; EDG5019724.1; -; Genomic_DNA.
DR EMBL; AAMEKY010000029; EDG5128692.1; -; Genomic_DNA.
DR EMBL; AAMEMC010000022; EDG5269037.1; -; Genomic_DNA.
DR EMBL; AAMEMH010000025; EDG5282468.1; -; Genomic_DNA.
DR EMBL; AAMEML010000041; EDG5291104.1; -; Genomic_DNA.
DR EMBL; AAMEMP010000037; EDG5372600.1; -; Genomic_DNA.
DR EMBL; DAAMEZ010000027; HAC6382089.1; -; Genomic_DNA.
DR EMBL; DAAMHM010000031; HAC6683519.1; -; Genomic_DNA.
DR EMBL; DAAQQK010000039; HAE0437519.1; -; Genomic_DNA.
DR EMBL; UGVQ01000002; SUE49318.1; -; Genomic_DNA.
DR RefSeq; WP_000866765.1; NZ_WFIN01000017.1.
DR AlphaFoldDB; A0A0T7RZR4; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000039541; Unassembled WGS sequence.
DR Proteomes; UP000254190; Unassembled WGS sequence.
DR Proteomes; UP000839929; 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; 3.40.50.20; -; 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}.
FT DOMAIN 109..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 429 AA; 45747 MW; 1571DDFD8E84B764 CRC64;
MKVLVIGNGG REHALAWKAA QSPLVDTVFV APGNAGTALE PALQNVAIGV TDIPALLSFA
QHEKIDLTIV GPEAPLVIGV VDAFRAAGLK IFGPTEGAAQ LEGSKAFTKD FLARHQIPTA
EYQNFTEIEP ALAYLREKGA PIVIKADGLA AGKGVIVAMT LEEAEAAVHD MLAGNAFGDA
GHRIVIEEFL DGEEASFIVM VDGEHVLPMA TSQDHKRVGN GDTGPNTGGM GAYSPAPVVT
DEVHQRTMER IIWPTVKGMA AEGNTYTGFL YAGLMIDKQG NPKVIEFNCR FGDPETQPIM
LRMKSDLVDL CLAACDGKLD EKTSEWDERA SLGVVIAAGG YPGNYNTGDE IHGLPLEEVA
DGKVFHAGTK LADDDRVLTS GGRVLCATAL GHTVAEAQKR AYALMTDIRW DGSFSRNDIG
WRAIEREQN
//