GUAAB_METAC
ID GUAAB_METAC Reviewed; 305 AA.
AC Q8THK3;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B;
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase;
GN Name=guaAB; Synonyms=guaA; OrderedLocusNames=MA_4511;
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., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2
CC H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase subunit
CC (A) and a GMP-binding subunit (B). {ECO:0000305}.
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DR EMBL; AE010299; AAM07851.1; -; Genomic_DNA.
DR RefSeq; WP_011024387.1; NC_003552.1.
DR AlphaFoldDB; Q8THK3; -.
DR SMR; Q8THK3; -.
DR STRING; 188937.MA_4511; -.
DR PRIDE; Q8THK3; -.
DR EnsemblBacteria; AAM07851; AAM07851; MA_4511.
DR GeneID; 1476405; -.
DR KEGG; mac:MA_4511; -.
DR HOGENOM; CLU_014340_0_0_2; -.
DR InParanoid; Q8THK3; -.
DR OMA; EGGIKSH; -.
DR OrthoDB; 31932at2157; -.
DR PhylomeDB; Q8THK3; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006177; P:GMP biosynthetic process; IBA:GO_Central.
DR CDD; cd01997; GMP_synthase_C; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00345; GMP_synthase_B; 1.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR026598; GMP_synthase_B.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; GMP biosynthesis; Ligase; Nucleotide-binding;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..305
FT /note="GMP synthase [glutamine-hydrolyzing] subunit B"
FT /id="PRO_0000140240"
FT DOMAIN 2..184
FT /note="GMPS ATP-PPase"
FT BINDING 29..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 305 AA; 34196 MW; 5D97F73EB1FC8251 CRC64;
MVKPEKFIPK AIEKISQEIK EGKAIIALSG GVDSSVCAEL AYRAIGDRLQ PIYIDTGLMR
KGETERIKHI FSHMNLHVVY AKDRFLEALA GVTDPEEKRK AVGETFIRVF EDEAKRIAAD
YLIQGTIYPD RIESEGGIKS HHNVGGLPSV MDFEKIVEPI EDLYKDEVRE VAWALQLPEE
ICERMPFPGP GLAVRILGEV TEEKLEVVRE ANFIVEEELL ERFCPWQTFA AVLGKGTGVK
GDIRAYGWIV AVRAVGSRDG MTAEALELPW EVLKHLEARI TSEIPKVARV VYDITPKPPA
TIEFE