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Database: UniProt
Entry: Q8TKT6
LinkDB: Q8TKT6
Original site: Q8TKT6 
ID   PUR2_METAC              Reviewed;         441 AA.
AC   Q8TKT6;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   16-JAN-2019, entry version 103.
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};
GN   OrderedLocusNames=MA_3309;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P.,
RA   FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A.,
RA   Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R.,
RA   Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W.,
RA   Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M.,
RA   Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A.,
RA   Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K.,
RA   Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C.,
RA   Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T.,
RA   Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E.,
RA   Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic
RT   and physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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 2 magnesium or manganese ions per subunit.
CC       {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}.
DR   EMBL; AE010299; AAM06679.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q8TKT6; -.
DR   SMR; Q8TKT6; -.
DR   STRING; 188937.MA3309; -.
DR   EnsemblBacteria; AAM06679; AAM06679; MA_3309.
DR   KEGG; mac:MA_3309; -.
DR   eggNOG; arCOG04415; Archaea.
DR   eggNOG; COG0151; LUCA.
DR   InParanoid; Q8TKT6; -.
DR   KO; K01945; -.
DR   OMA; KATVCKY; -.
DR   PhylomeDB; Q8TKT6; -.
DR   UniPathway; UPA00074; UER00125.
DR   Proteomes; UP000002487; 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    441       Phosphoribosylamine--glycine ligase.
FT                                /FTId=PRO_0000151509.
FT   DOMAIN      112    319       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00138}.
FT   NP_BIND     139    196       ATP. {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       277    277       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       289    289       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       289    289       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
FT   METAL       291    291       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00138}.
SQ   SEQUENCE   441 AA;  47750 MW;  CDC8AF5A3B9C4C9C CRC64;
     MKMKILLIGG GGREHAIAEG IKESKHNPIL YALMAKKNPG IAALCEDFLL EKETEVEKIV
     EYAKARNIEM AFVGPEAPLA AGVADALWEA GIPVVGPKKA CAVIEFDKAW ARNFMKKYGI
     EGCPAYEVFT EEAPAHAFIE KLGDVAVKPS GLTGGKGVKV MGDQLPDLKA AKDYTSELLE
     KGPVVIEERF IGEEFTLQAF VDGKNLAFFP AVQDHKRAYE GDLGPNTGGM GSYTDAGEIL
     PFMLAGDIEQ AKKIMQHTVT ALHEETGTGY QGVLYGQFIL TASGPKVVEF NARFGDPEAM
     NVIPLIETDF TEIMSAVVKS TLDSLPVKFS RKATVCKYAV PAGYPDNPEK DSEVLVGDVG
     EASVYYASVY EKEGKIYTTG SRAVAVVGRA ETIDAAEKIA QNALENIQGK LFFRKDIGTA
     SLIQKRIDHM KELRGGLSQK Q
//
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