ID D2QJG3_SPILD Unreviewed; 510 AA.
AC D2QJG3;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 91.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|HAMAP-Rule:MF_00344};
DE EC=6.3.5.2 {ECO:0000256|HAMAP-Rule:MF_00344};
DE AltName: Full=GMP synthetase {ECO:0000256|HAMAP-Rule:MF_00344};
DE AltName: Full=Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00344};
GN Name=guaA {ECO:0000256|HAMAP-Rule:MF_00344};
GN OrderedLocusNames=Slin_2862 {ECO:0000313|EMBL:ADB38876.1};
OS Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896 / Claus 1).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=504472 {ECO:0000313|EMBL:ADB38876.1, ECO:0000313|Proteomes:UP000002028};
RN [1] {ECO:0000313|Proteomes:UP000002028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896
RC {ECO:0000313|Proteomes:UP000002028};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Mikhailova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindal B., Schutze A., Schneider S.,
RA Goker M., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Spirosoma linguale DSM 74.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADB38876.1, ECO:0000313|Proteomes:UP000002028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896
RC {ECO:0000313|Proteomes:UP000002028};
RX PubMed=21304700;
RA Lail K., Sikorski J., Saunders E., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.-F., Lucas S., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J.,
RA Jeffries C.D., Chain P., Brettin T., Detter J.C., Schuetze A., Rohde M.,
RA Tindall B.J., Goeker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.-P., Chen F.;
RT "Complete genome sequence of Spirosoma linguale type strain (1).";
RL Stand. Genomic Sci. 2:176-185(2010).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC {ECO:0000256|ARBA:ARBA00002332, ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_00344};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00005153, ECO:0000256|HAMAP-
CC Rule:MF_00344}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00344}.
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DR EMBL; CP001769; ADB38876.1; -; Genomic_DNA.
DR AlphaFoldDB; D2QJG3; -.
DR STRING; 504472.Slin_2862; -.
DR MEROPS; C26.957; -.
DR KEGG; sli:Slin_2862; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_10; -.
DR OMA; DQLTCMF; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000002028; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR Gene3D; 3.30.300.10; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00884; guaA_Cterm; 1.
DR NCBIfam; TIGR00888; guaA_Nterm; 1.
DR PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00958; GMP_synt_C; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00344};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_00344};
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP-
KW Rule:MF_00344};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00344};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00344};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00344}.
FT DOMAIN 195..385
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 168
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 170
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 222..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 510 AA; 55661 MW; C9F2E57214A43AAF CRC64;
MATEQILILD FGSQYTQLIA RRVRELNVYC EIHPYNHLPT ITPDVKGIIL SGSPSSVRDA
DAPDVHLAAF RHKMPLLGIC YGAQLLAHTN GGEVKASAIR EYGRAKLGTV DGESPLLKGI
DPHSQVWMSH ADTITSVPEN FSIIASTDTV HVAAFQVDNE PTYGIQFHPE VTHSLQGKML
LHNFVVDICG CSQNWTAESF AETTIAQLKQ KLGDDKVVLG LSGGVDSSVA AMLIHQAIGK
NLYCIFVDNG LLRKDEFLGV LDSYKTLGLN VKGVDAKDQF YTALAGLTDP EAKRKAIGKT
FIDVFDHEAH LIEGVSWLGQ GTIYPDVIES VSVKGPSATI KSHHNVGGLP DFMKLKVVEP
LNTLFKDEVR AVGRTLGLPD AILGRHPFPG PGLAIRILGD ITPEKVDILQ QVDALFIDGL
KREGLYDKVW QAGAMLLPVQ SVGVMGDERT YERVVALRAV TSVDGMTADW AHLPYEFLAD
VSNEIINRVK GVNRVVYDIS SKPPATIEWE
//