ID A0A485AXN1_KLUCR Unreviewed; 253 AA.
AC A0A485AXN1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 02-APR-2025, entry version 28.
DE RecName: Full=GMP synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012746};
DE EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
GN Name=guaA_2 {ECO:0000313|EMBL:VFS64058.1};
GN ORFNames=NCTC12993_03061 {ECO:0000313|EMBL:VFS64058.1};
OS Kluyvera cryocrescens (Kluyvera citrophila).
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Enterobacteriaceae; Kluyvera.
OX NCBI_TaxID=580 {ECO:0000313|EMBL:VFS64058.1, ECO:0000313|Proteomes:UP000401081};
RN [1] {ECO:0000313|EMBL:VFS64058.1, ECO:0000313|Proteomes:UP000401081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12993 {ECO:0000313|EMBL:VFS64058.1,
RC ECO:0000313|Proteomes:UP000401081};
RG Pathogen Informatics;
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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:PRU00886}.
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DR EMBL; CAADJD010000018; VFS64058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A485AXN1; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000401081; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR CDD; cd01997; GMP_synthase_C; 1.
DR FunFam; 3.30.300.10:FF:000002; GMP synthase [glutamine-hydrolyzing]; 1.
DR Gene3D; 3.30.300.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
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; PF00958; GMP_synt_C; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:VFS64058.1};
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:UP000401081}.
FT DOMAIN 1..125
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
SQ SEQUENCE 253 AA; 28675 MW; 5847D249B15ABB11 CRC64;
MFGDHFGLNI VHVEGEKRFL DALAGENDPE AKRKIIGRVF VEVFDEEALK LEDVKWLAQG
TIYPDVIESA ASATGKAHVI KSHHNVGGLP KEMKMGLVEP LRELFKDEVR KIGLELGLPY
DMLYRHPFPG PGLGVRVLGE VKKEYCDLLR RADAIFIEEL HKADLYNKVS QAFTVFLPVR
SVGVMGDGRK YDWVVSLRAV ETIDFMTAHW AHLPYDFLGR VSKPHHQRSE QHFPAWFMTS
AASHRQRSSG NDV
//
