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Database: UniProt
Entry: Q7UPZ8
LinkDB: Q7UPZ8
Original site: Q7UPZ8 
ID   PUR2_RHOBA              Reviewed;         437 AA.
AC   Q7UPZ8;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   16-JAN-2019, entry version 91.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000255|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000255|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000255|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000255|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000255|HAMAP-Rule:MF_00138}; OrderedLocusNames=RB6616;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T.,
RA   Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R.,
RA   Schlesner H., Amann R., Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp.
RT   strain 1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58089,
CC         ChEBI:CHEBI:58457, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00138};
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;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-diphosphate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00138}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD74908.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; BX294144; CAD74908.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_867362.1; NC_005027.1.
DR   ProteinModelPortal; Q7UPZ8; -.
DR   SMR; Q7UPZ8; -.
DR   STRING; 243090.RB6616; -.
DR   PRIDE; Q7UPZ8; -.
DR   EnsemblBacteria; CAD74908; CAD74908; RB6616.
DR   GeneID; 1795089; -.
DR   KEGG; rba:RB6616; -.
DR   PATRIC; fig|243090.15.peg.3204; -.
DR   eggNOG; ENOG4107QNG; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033463; -.
DR   InParanoid; Q7UPZ8; -.
DR   KO; K01945; -.
DR   OrthoDB; 932854at2; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000001025; 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   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; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    437       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151475.
FT   DOMAIN      110    322       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     142    203       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       292    292       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       294    294       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
SQ   SEQUENCE   437 AA;  46501 MW;  FF709E7F10A19993 CRC64;
     MSKYNVLIVG SGGREHALAW KVKQSQHVQN VFVAPGNAGT GMDATNVDLD PADHDAVIQF
     AKENNVGLVI VGPEAPLVAG LVDALTDAGL RAFGPSKAAS ELEGSKVFCK NLLRSADIPT
     ADYRTFRSAD DASRYIKDRF SEPTDPVNVV VKADGLAAGK GVVVCDTRSE ALEAIDRIAA
     RKEFGAAGKE LIIEERLTGP EVSVLAITDG ETIVTLPPAQ DHKPANDGDT GPNTGGMGAY
     CPAPVLDEET LAKVESSILV PVVHAMKRSR RPFKGVLYAG LMLTPAGPKV LEFNVRFGDP
     ECQPLLMRLK TDLVEVMQAV VDGKLEETGP LEFDPRPAIC VVMASEGYPA DYEKGHAITG
     IESADKMENV KVFHAGTQRV DGEVVNTGGR VLGVTAMGDS ISAAKLQAYK AVREIRWQGA
     WCRKDISDKA LVTADKA
//
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