ID A0A444H9W9_9FLAO Unreviewed; 425 AA.
AC A0A444H9W9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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:RWX00051.1};
GN ORFNames=EPI11_10940 {ECO:0000313|EMBL:RWX00051.1};
OS Flavobacterium cerinum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2502784 {ECO:0000313|EMBL:RWX00051.1, ECO:0000313|Proteomes:UP000287527};
RN [1] {ECO:0000313|EMBL:RWX00051.1, ECO:0000313|Proteomes:UP000287527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1E403 {ECO:0000313|EMBL:RWX00051.1,
RC ECO:0000313|Proteomes:UP000287527};
RA Zhang R., Du Z.-J.;
RT "Flavobacterium sp. nov.,isolated from freshwater.";
RL Submitted (JAN-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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWX00051.1}.
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DR EMBL; SBII01000007; RWX00051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444H9W9; -.
DR OrthoDB; 9807240at2; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000287527; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000287527}.
FT DOMAIN 111..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 425 AA; 46148 MW; 139725570D68BE69 CRC64;
MKILLLGSGG REHALAWKML QSPSCDKLFV APGNAGTAGI ASNVNINPLD FESIKAFVQQ
EDINMVVVGP EDPLVKGIYD YFKKDEALKD IPVIGPSKNG AQLEGSKEFA KQFLIKNNIP
TAAYDSFTKE TVEQGCEFLT TLQPPYVLKA DGLAAGKGVL ILESLAEAQQ ELRNMLVGEK
FGQASTKVVI EEFLDGIELS CFVLTDGKSY KLLPTAKDYK RIGEGDTGLN TGGMGAVSPV
PFADAVFMEK IETRIVKPTI EGLNSGGIEY KGFVFIGIIK VGDDPFVIEY NVRMGDPETE
VVIPRLKSDL VELFTAVANQ ELDKVTLEID ERSAATIMVV SGGYPEDYGK GMIISGLDAV
EGSIAFHAGT KLDGNNNVVT SGGRVIAVTS YGKDFDEAIK KSYQNIDKLN FDKMYYRKDI
GFDLR
//
