ID C7C0C3_HELPB Unreviewed; 424 AA.
AC C7C0C3;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
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:CAX29888.1};
GN OrderedLocusNames=HELPY_1194 {ECO:0000313|EMBL:CAX29888.1};
OS Helicobacter pylori (strain B38).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=592205 {ECO:0000313|EMBL:CAX29888.1, ECO:0000313|Proteomes:UP000000313};
RN [1] {ECO:0000313|EMBL:CAX29888.1, ECO:0000313|Proteomes:UP000000313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B38 {ECO:0000313|EMBL:CAX29888.1,
RC ECO:0000313|Proteomes:UP000000313};
RX PubMed=20537153; DOI=10.1186/1471-2164-11-368;
RA Thiberge J.M., Boursaux-Eude C., Lehours P., Dillies M.A., Creno S.,
RA Coppee J.Y., Rouy Z., Lajus A., Ma L., Burucoa C., Ruskone-Foumestraux A.,
RA Courillon-Mallet A., De Reuse H., Boneca I.G., Lamarque D., Megraud F.,
RA Delchier J.C., Medigue C., Bouchier C., Labigne A., Raymond J.;
RT "From array-based hybridization of Helicobacter pylori isolates to the
RT complete genome sequence of an isolate associated with MALT lymphoma.";
RL BMC Genomics 11:368-368(2010).
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 -!- 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; FM991728; CAX29888.1; -; Genomic_DNA.
DR RefSeq; WP_000654411.1; NC_012973.1.
DR AlphaFoldDB; C7C0C3; -.
DR KEGG; hpb:HELPY_1194; -.
DR HOGENOM; CLU_027420_3_0_7; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000000313; 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; 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.
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 111..312
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 424 AA; 47428 MW; 33AD6C115235F96B CRC64;
MKDNNNYNVL IVGNKGREYA LAQRLQQDER VNALYFCLGN GGTQDLGENL ECEHYEHIVE
LALKKQIHLA IISEEELLVL GLTEMLEKAG ILVFGASKEA AKLEASKSYM KAFVKECGIK
SASYFETNDL KEALSYIQNA SFPLVVKALN KNTSIVHQQE EALKILEDAF KQSNEPVIIE
PFLEGFELSV TALIANDDFI LLPFCQNYKR LLEGDNGVNT GGMGAIAPAN FFSNELEEKI
KNHIFKPTLE KLQANNTPFK GVLLAEIVII EEKGVLEPYL LDFSVRFKDI ECQTILPLLE
SSLLDLCLAT AKGELHSLEL VFSKEFVMSV ALVSRNYPTS SSPKQTLYID PVDEKKGHLI
LGEVEQDNGV FESSGGRVIF AIGRGKSLLE ARNHAYEIAQ KVHFEGMFYR KDIGFKVLDL
KEYS
//
