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Database: UniProt
Entry: C4ZNN8_THASP
LinkDB: C4ZNN8_THASP
Original site: C4ZNN8_THASP 
ID   C4ZNN8_THASP            Unreviewed;       426 AA.
AC   C4ZNN8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   05-JUN-2019, entry version 68.
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   OrderedLocusNames=Tmz1t_1442 {ECO:0000313|EMBL:ACK54201.1};
OS   Thauera sp. (strain MZ1T).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Zoogloeaceae; Thauera.
OX   NCBI_TaxID=85643 {ECO:0000313|EMBL:ACK54201.1, ECO:0000313|Proteomes:UP000002186};
RN   [1] {ECO:0000313|Proteomes:UP000002186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sayler G.S.;
RT   "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACK54201.1, ECO:0000313|Proteomes:UP000002186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZ1T {ECO:0000313|EMBL:ACK54201.1,
RC   ECO:0000313|Proteomes:UP000002186};
RX   PubMed=23407619; DOI=10.4056/sigs.2696029;
RA   Jiang K., Sanseverino J., Chauhan A., Lucas S., Copeland A.,
RA   Lapidus A., Del Rio T.G., Dalin E., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Chang Y.J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N.C., Mikhailova N.,
RA   Moser S., Jegier P., Close D., Debruyn J.M., Wang Y., Layton A.C.,
RA   Allen M.S., Sayler G.S.;
RT   "Complete genome sequence of Thauera aminoaromatica strain MZ1T.";
RL   Stand. Genomic Sci. 6:325-335(2012).
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; CP001281; ACK54201.1; -; Genomic_DNA.
DR   RefSeq; WP_004308702.1; NC_011662.2.
DR   STRING; 85643.Tmz1t_1442; -.
DR   EnsemblBacteria; ACK54201; ACK54201; Tmz1t_1442.
DR   KEGG; tmz:Tmz1t_1442; -.
DR   eggNOG; ENOG4105C12; Bacteria.
DR   eggNOG; COG0151; LUCA.
DR   HOGENOM; HOG000033463; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   OrthoDB; 932854at2; -.
DR   BioCyc; TSP85643:TMZ1T_RS07095-MONOMER; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000002186; 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; 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:UP000002186};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00138, ECO:0000313|EMBL:ACK54201.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002186}.
FT   DOMAIN      107    314       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION      211    233       Disordered. {ECO:0000256|MobiDB-lite:
FT                                C4ZNN8}.
SQ   SEQUENCE   426 AA;  45061 MW;  95D64039360845D4 CRC64;
     MKVLVIGSGG REHALAWKLA QSPKVTRVLV APGNPGTAAE KLLQNVPVTD IKVLVELAKH
     EHVAFTVVGP EAPLAAGVVD AFRAAGLPIF GPTKAAAQLE SSKDFAKQFL VRHNIPTAKY
     QTFADAAAAH AYVDAEGAPI VIKADGLAAG KGVVVAMTAD EAHAAIDMML LDNRMGDAGA
     RVVIEEFMEG EEASFIVMAD GKHALALATS QDHKRLHDGD QGPNTGGMGA YSPAPVVTPD
     VHARVMREVI NPTLTGMAAE GLPYTGFLYA GLMIDGEGKP RVVEFNCRMG DPETQPIMMR
     LKTDLADLIE AAIAGKLDQT EAEWDRRFAL GVVLAAAGYP ESPRKGDVIT GLPASEQEDV
     HVFHAGTALQ DSQVVTAGGR VLCVTALGDN VRSAQKRAYE VADGIVFEGR QYRRDIGHRA
     IGRKTA
//
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