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Database: UniProt
Entry: C9ZDQ0_STRSW
LinkDB: C9ZDQ0_STRSW
Original site: C9ZDQ0_STRSW 
ID   C9ZDQ0_STRSW            Unreviewed;       417 AA.
AC   C9ZDQ0;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000256|HAMAP-Rule:MF_00138};
DE            EC=6.3.4.13 {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=GARS {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
DE   AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000256|HAMAP-Rule:MF_00138};
GN   Name=purD {ECO:0000256|HAMAP-Rule:MF_00138,
GN   ECO:0000313|EMBL:CBG71824.1};
GN   OrderedLocusNames=SCAB_47701 {ECO:0000313|EMBL:CBG71824.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG71824.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG71824.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG71824.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H.,
RA   Parry R.J., Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like
RT   biosynthetic cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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:0000256|HAMAP-Rule:MF_00138};
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:0000256|HAMAP-Rule:MF_00138}.
CC   -!- SIMILARITY: Belongs to the GARS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00138}.
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DR   EMBL; FN554889; CBG71824.1; -; Genomic_DNA.
DR   RefSeq; WP_013002414.1; NC_013929.1.
DR   STRING; 680198.SCAB_47701; -.
DR   EnsemblBacteria; CBG71824; CBG71824; SCAB_47701.
DR   GeneID; 24309665; -.
DR   KEGG; scb:SCAB_47701; -.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033463; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   OrthoDB; 932854at2; -.
DR   BioCyc; SSCA680198:G1GK9-4666-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000001444; 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; 3.30.1490.20; -; 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 {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001444};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:CBG71824.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT   DOMAIN      107    303       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   417 AA;  42566 MW;  76B3F99E9BE0B910 CRC64;
     MKVLVIGSGA REHALCRSLS LDPDVTALHC APGNAGTAEV AESHPVDALD GAAVTALATR
     LEADLVVVGP EAPLVAGVAD AVRAAGIPVF GPSGEAAQLE GSKAFAKEVM AGAGVPTARS
     YVCTTAEEID EALDAFGAPY VVKDDGLAAG KGVVVTADLA QAREHALACG RVVIEEFLDG
     PEVSLFAITD GVTVVPLQPA QDFKRALDGD EGPNTGGMGA YSPLPWADPK LVDEVLQSVL
     QPTVDEMRRR GTPFSGLLYA GLAITGRGVR VIEFNARFGD PETQVVLARL KTPLAGVLLA
     AANGTLGDLE PLRWSADAAV TVVVASHNYP GSPRTGDPVT GLDEVAAVDA PHAYVLHAGT
     KLAGDEVVSA GGRVLSVTAT GKDLTQARDR AYTAVARIGL DGSQHRSDIA AKAAAEA
//
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