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Database: UniProt
Entry: V9H4I3_9CLOT
LinkDB: V9H4I3_9CLOT
Original site: V9H4I3_9CLOT 
ID   V9H4I3_9CLOT            Unreviewed;       415 AA.
AC   V9H4I3;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   08-MAY-2019, entry version 33.
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   ORFNames=CSBG_02305 {ECO:0000313|EMBL:EEH98679.1};
OS   Clostridium sp. 7_2_43FAA.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=457396 {ECO:0000313|EMBL:EEH98679.1, ECO:0000313|Proteomes:UP000017809};
RN   [1] {ECO:0000313|EMBL:EEH98679.1, ECO:0000313|Proteomes:UP000017809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7_2_43FAA {ECO:0000313|EMBL:EEH98679.1,
RC   ECO:0000313|Proteomes:UP000017809};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E.,
RA   Strauss J., Ambrose C., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium sp. 7_2_43FAA.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EEH98679.1}.
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DR   EMBL; ACDK02000013; EEH98679.1; -; Genomic_DNA.
DR   RefSeq; WP_008677542.1; NZ_JH815222.1.
DR   STRING; 457396.CSBG_02305; -.
DR   EnsemblBacteria; EEH98679; EEH98679; CSBG_02305.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   BioCyc; GCF_000158375-HMP:CSBG_RS04795-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000017809; 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; 3.30.1490.20; -; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Complete proteome {ECO:0000313|Proteomes:UP000017809};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:EEH98679.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017809}.
FT   DOMAIN      107    313       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
SQ   SEQUENCE   415 AA;  45745 MW;  0CEDED5FB984F876 CRC64;
     MKILLIGSGG REHAIAWKLS KNEKVEKIFV APGNGGTARE SKCENVNIIE IDQLLEFALE
     NFIDLTVVGP EDPLTRGIVD KFKMNGLKIF GPSKKAAMLE GSKSFSKDFM KKYGVKTAEY
     EVFYDVNKAL NYLEKCPYPT VVKADGLAAG KGVAICNDKE EAIAAVKSFM VDDIFNGAGQ
     KIIIEEFLEG VEASILSITD GKTIIPFISA KDHKQIFDGG KGPNTGGMGV VAPNPYVTEE
     VLKDFEENIM NRTLVGIREE GFDYKGIIFF GIMITKKGSY LLEYNVRMGD PETQSVLNLM
     ESDLLELIEA SLIEDLKNTE VKWKNGACVN VVLSSKGYPG SFTKGYEITI DDDIKDKVFL
     AGAKLENEIL KTNGGRVLSV VGVGETIEKA RKDAYKTIEK VEFKDKYFRN DIGLV
//
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