ID X5GXH8_9RICK Unreviewed; 519 AA.
AC X5GXH8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=GMP synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012746};
DE EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746};
GN Name=guaA {ECO:0000313|EMBL:AHX11762.1};
GN ORFNames=NHE_0842 {ECO:0000313|EMBL:AHX11762.1};
OS Neorickettsia helminthoeca str. Oregon.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Neorickettsia.
OX NCBI_TaxID=1286528 {ECO:0000313|EMBL:AHX11762.1, ECO:0000313|Proteomes:UP000023755};
RN [1] {ECO:0000313|EMBL:AHX11762.1, ECO:0000313|Proteomes:UP000023755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon {ECO:0000313|EMBL:AHX11762.1,
RC ECO:0000313|Proteomes:UP000023755};
RA Lin M., Daugherty S.C., Nagaraj S., Cheng Z., Xiong Q., Lin F.-Y.,
RA Sengamalay N., Ott S., Godinez A., Tallon L.J., Sadzewicz L., Fraser C.M.,
RA Dunning Hotopp J.C., Rikihisa Y.;
RT "Sequencing and Comparison of Genomes and Transcriptome Profiles of Human
RT Ehrlichiosis Agents.";
RL Submitted (MAR-2014) 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}.
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DR EMBL; CP007481; AHX11762.1; -; Genomic_DNA.
DR RefSeq; WP_038560127.1; NZ_CP007481.1.
DR AlphaFoldDB; X5GXH8; -.
DR STRING; 1286528.NHE_0842; -.
DR KEGG; nhm:NHE_0842; -.
DR HOGENOM; CLU_014340_0_5_5; -.
DR OrthoDB; 9802219at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000023755; 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 InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR001674; GMP_synth_C.
DR InterPro; IPR004739; GMP_synth_GATase.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
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 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 ECO:0000256|PROSITE-ProRule:PRU00605};
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|PROSITE-
KW ProRule:PRU00886};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AHX11762.1};
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:UP000023755}.
FT DOMAIN 197..385
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 173
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 224..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 519 AA; 58184 MW; EC61A86575B6A5FE CRC64;
MTSQIAIIDL GSQFTQLIAR KLRENKCYSQ IYSPEGFVFS SAMKGIILSG SHKSIDEYVH
YRDLVSEILD VNSRYGVPVL GICYGKQLIS DFFGARVVSG EKREYGKAEL QITGESLITE
NIKERSFTVW MSHGDTVATV PDGFRGIART EDCEFAVIAN DQKKLYGFQF HPEVSHSENG
EILLRNFIEI SRAANTWDLQ IFSNQEKRQI IQSVGESHVL AAVSGGVDST VAAKFMYEAI
GSRLHCIFVD TGLLRKNEVD EVKKSFFLLG IPLEVISASH QFFDRLACIT EPEEKRKIIG
ETFINVFESK ASTIENVEFL LQGTLYPDIV ESGVSGSHAI KSHHNVGGLP VKMGLKLLEP
FRLLFKDEVR AIGRNMGVDE TILMRHPSPG PGLAIRILGE VTEEKVRILQ NVDDIYLSTM
RRYGLYSKIW QAFTVLLPIR SVGVMGDKRS YNYVCAVRAV TSRDGMTASA YPFESDSSDK
ILFLEFLNEI ATKIPNQVKE VSRIVYDITS KPPATIEWE
//
