PUR2_ALLVD
ID PUR2_ALLVD Reviewed; 428 AA.
AC Q46482; D3RQG2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Phosphoribosylamine--glycine ligase;
DE EC=6.3.4.13;
DE AltName: Full=GARS;
DE AltName: Full=Glycinamide ribonucleotide synthetase;
DE AltName: Full=Phosphoribosylglycinamide synthetase;
GN Name=purD; OrderedLocusNames=Alvin_0820;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-189.
RA Chen Y.L., Knaff D.B.;
RL Submitted (APR-1996) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
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.
CC -!- SIMILARITY: Belongs to the GARS family. {ECO:0000305}.
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DR EMBL; CP001896; ADC61767.1; -; Genomic_DNA.
DR EMBL; L76417; AAB02980.1; -; Genomic_DNA.
DR RefSeq; WP_012970043.1; NC_013851.1.
DR AlphaFoldDB; Q46482; -.
DR SMR; Q46482; -.
DR STRING; 572477.Alvin_0820; -.
DR EnsemblBacteria; ADC61767; ADC61767; Alvin_0820.
DR KEGG; alv:Alvin_0820; -.
DR eggNOG; COG0151; Bacteria.
DR HOGENOM; CLU_027420_3_1_6; -.
DR OMA; KATVCKY; -.
DR OrthoDB; 932854at2; -.
DR UniPathway; UPA00074; UER00125.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.30.1490.20; -; 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; 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 PANTHER; PTHR43472; PTHR43472; 1.
DR Pfam; PF01071; GARS_A; 1.
DR Pfam; PF02843; GARS_C; 1.
DR Pfam; PF02844; GARS_N; 1.
DR SMART; SM01210; GARS_C; 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; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..428
FT /note="Phosphoribosylamine--glycine ligase"
FT /id="PRO_0000151443"
FT DOMAIN 109..316
FT /note="ATP-grasp"
FT REGION 211..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 95..97
FT /note="RQA -> ASG (in Ref. 2; AAB02980)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..160
FT /note="DD -> MI (in Ref. 2; AAB02980)"
FT /evidence="ECO:0000305"
FT CONFLICT 165..167
FT /note="EAA -> GGG (in Ref. 2; AAB02980)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..183
FT /note="GGRFGRAGAR -> ADAFGPGGGG (in Ref. 2; AAB02980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 44805 MW; 3CBFD73C9F913D37 CRC64;
MKILIVGSGG REHALAWKAA QSPQVEQVFV APGNGGTASE PGVENVAIAA DDIAGLVEFA
RRESIGLTIV GPEAPLVLGL VDAFAEAGLP CFGPRQASAQ LEGSKAFAKD FLHRHGIPTA
AYGVFTELEP ALAYLRQVGA PVVVKADGLA AGKGVILADD LATAEAAVHD MLGGGRFGRA
GARVVIEEFL TGEEASFIAM VDGRHILPLA SSQDHKARDD GDRGPNTGGM GAYSPAPIVT
PEIHDRIMRE VMEPTVAGLA AEGLPYLGFL YAGLMIGADG TPKVLEFNCR LGDPETQPLL
MRLQSDLVEL CLAALDGRLD QVTADWDARP ALGVVMAAGG YPDDYETGHV ISGLDAVPSS
EAKVFQAGTR CEGDAILTNG GRVLCVTALG ANVAEAQHLA YQAVDRIQWT DAFCRRDIGH
RAIARERS
