GUAA_COXBU
ID GUAA_COXBU Reviewed; 524 AA.
AC Q83BZ6;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=CBU_1341;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO90844.1; -; Genomic_DNA.
DR RefSeq; NP_820330.1; NC_002971.3.
DR RefSeq; WP_010958163.1; NC_002971.4.
DR PDB; 3TQI; X-ray; 2.84 A; A/B/C/D=1-524.
DR PDBsum; 3TQI; -.
DR AlphaFoldDB; Q83BZ6; -.
DR SMR; Q83BZ6; -.
DR STRING; 227377.CBU_1341; -.
DR DNASU; 1209247; -.
DR EnsemblBacteria; AAO90844; AAO90844; CBU_1341.
DR GeneID; 1209247; -.
DR KEGG; cbu:CBU_1341; -.
DR PATRIC; fig|227377.7.peg.1333; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR HOGENOM; CLU_014340_0_5_6; -.
DR OMA; KRKIIGH; -.
DR UniPathway; UPA00189; UER00296.
DR EvolutionaryTrace; Q83BZ6; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006177; P:GMP biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glutamine amidotransferase; GMP biosynthesis;
KW Ligase; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..524
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140120"
FT DOMAIN 9..207
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT DOMAIN 208..399
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 181
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT ACT_SITE 183
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT BINDING 235..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3TQI"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:3TQI"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:3TQI"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 211..225
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:3TQI"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 304..321
FT /evidence="ECO:0007829|PDB:3TQI"
FT TURN 322..327
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 337..341
FT /evidence="ECO:0007829|PDB:3TQI"
FT TURN 374..377
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 380..390
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 418..435
FT /evidence="ECO:0007829|PDB:3TQI"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 443..455
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 466..474
FT /evidence="ECO:0007829|PDB:3TQI"
FT HELIX 489..502
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:3TQI"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:3TQI"
FT TURN 516..518
FT /evidence="ECO:0007829|PDB:3TQI"
SQ SEQUENCE 524 AA; 58682 MW; F45A43498D93317D CRC64;
MLKDIHQHRI LILDFGSQYA QLIARRVREI GVYCELMPCD IDEETIRDFN PHGIILSGGP
ETVTLSHTLR APAFIFEIGC PVLGICYGMQ TMAYQLGGKV NRTAKAEFGH AQLRVLNPAF
LFDGIEDQVS PQGEPLLDVW MSHGDIVSEL PPGFEATACT DNSPLAAMAD FKRRFFGLQF
HPEVTHTPQG HRILAHFVIH ICQCIPNWTT KHIIEDSIRD IQEKVGKEQV IVGLSGGVDS
AVTATLVHKA IGDQLVCVLV DTGLLRLNEV DEVLNVFQKH LGAKVICVDA KDRFMKALKG
ISDPEEKRKI AGEQFIRVFE EQAKKLNVKW LGQGTIYPDV IESAKTKTGK GHIIKTHHNV
GGLPLNMELK LIEPLRELFK DEVRKLGLEL GLPADLIYRH PFPGPGLAIR ILGEVSAEYI
NILKQADAIF IEELKKSDYY HQVSQAFAVF MPLKSVGVKG DARHYGYIIA LRAVKTVDFM
TAQWADLPHE FLSKVSHRIV NEIKEVSRVV YDMTNKPPAT IEWE
