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Database: UniProt
Entry: F3KD58_9GAMM
LinkDB: F3KD58_9GAMM
Original site: F3KD58_9GAMM 
ID   F3KD58_9GAMM            Unreviewed;       413 AA.
AC   F3KD58;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|ARBA:ARBA00021562};
DE            EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00031356};
GN   ORFNames=imdm_802 {ECO:0000313|EMBL:EGG99696.1};
OS   gamma proteobacterium IMCC2047.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=434085 {ECO:0000313|EMBL:EGG99696.1, ECO:0000313|Proteomes:UP000004485};
RN   [1] {ECO:0000313|EMBL:EGG99696.1, ECO:0000313|Proteomes:UP000004485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=imcc2047 {ECO:0000313|Proteomes:UP000004485};
RX   PubMed=21602327; DOI=10.1128/JB.05226-11;
RA   Kang I., Kang D., Oh H.M., Kim H., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.;
RT   "Genome sequence of strain IMCC2047, a novel marine member of the
RT   Gammaproteobacteria.";
RL   J. Bacteriol. 193:3688-3689(2011).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC       {ECO:0000256|ARBA:ARBA00002332}.
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00005153}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGG99696.1}.
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DR   EMBL; AEGL01000187; EGG99696.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3KD58; -.
DR   PATRIC; fig|434085.3.peg.685; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000004485; Unassembled WGS sequence.
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-KW.
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   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR001674; GMP_synth_C.
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   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   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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00886};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|PROSITE-
KW   ProRule:PRU00886}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00886};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|PROSITE-
KW   ProRule:PRU00886}; Reference proteome {ECO:0000313|Proteomes:UP000004485}.
FT   DOMAIN          96..288
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   BINDING         123..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   413 AA;  45996 MW;  4166BD0E0DB480DB CRC64;
     MKVDTPSRLL EGIADHTDEA GNVLLDVWMS HGDKVTQLPE GFEVMASTGS APIAGMCDDS
     RAFYGVQFHP EVTHTLQGLR LLEHFVKNIA GCEGLWTPAQ IIEDAIDTVR KQVGTDHVLL
     GLSGGVDSSV VAALLHRAIG DQLTCVFVDN GLLRKNEGDQ VMDMFGKNMG VRVIRADAEE
     LFLSRLKGEN DPEKKRKIIG NTFIEVFDEE SSKIDNVKWL AQGTIYPDVI ESAAAKTGKA
     HVIKSHHNVG GLPEDMKLGL VEPLRELFKD EVRKIGLELG LPYDMVYRHP FPGPGLGVRI
     LGEIKKEYAD ILREADAIFI EELHNFDYYH KTSQAFTVFL PVKSVGVVGD QRQYEYVVAI
     RAVETIDFMT ARWAHLPYEL LEKVSSRIIN EVKGISRVTY DISSKPPATI EWE
//
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