GUAA_CARHZ
ID GUAA_CARHZ Reviewed; 509 AA.
AC Q3AD70;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_00344};
DE EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00344};
DE AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00344};
DE AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_00344};
GN Name=guaA {ECO:0000255|HAMAP-Rule:MF_00344}; OrderedLocusNames=CHY_1068;
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(2005).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC Rule:MF_00344}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00344};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00344}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00344}.
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DR EMBL; CP000141; ABB15970.1; -; Genomic_DNA.
DR RefSeq; WP_011343990.1; NC_007503.1.
DR AlphaFoldDB; Q3AD70; -.
DR SMR; Q3AD70; -.
DR STRING; 246194.CHY_1068; -.
DR MEROPS; C26.A21; -.
DR EnsemblBacteria; ABB15970; ABB15970; CHY_1068.
DR KEGG; chy:CHY_1068; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_9; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 504464at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000002706; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00344; GMP_synthase; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR004739; GMP_synth_GATase.
DR InterPro; IPR022955; GMP_synthase.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..509
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000229416"
FT DOMAIN 4..194
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 195..384
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 168
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 170
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 222..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ SEQUENCE 509 AA; 57147 MW; 794E777F80D102F1 CRC64;
MASKVIVLDF GGQYSQLIAR RIRELKVYCE MLPYNTPLEK IVQENPGGIV FSGGPSSVYG
EGAPTVDPEI YRLNIPILGI CYGMQLMAHQ LGGIVRPAEG REYGKTPLFI LNRDRLFAGL
NETEICWMSH GDFVAKAPEG FLVTAKTEYT PIAAMENRER NLYAVQFHPE VVHTPKGKEI
LKNFLYEICG LTPDWTMESF AQKAIREIKE QVGEEKVVCA LSGGVDSSVA AVLVHKAIGD
NLTCIFVDHG LLRKGEAEEV VRTFKEQFQM NLVFVDAKEQ FLAKLKGVRD PEQKRKIIGH
EFIRVFEEEA AKLGDIRFLV QGTLYPDVVE SGTATAATIK SHHNVGGLPE DMKFQLIEPL
KWLFKDEVRE LGLELGLPES IVWRHPFPGP GLAVRVLGEI TEEKLAILRE ADYIFIDELK
KSGWYRKTWQ AFAVLPNLQS VGVMGDERTY AYTIALRAVT SEDGMTADWV RLPYELLEKI
SARIVGEVKG VNRVVYDITS KPPATIEWE
