位置:首页 > 蛋白库 > GUAA_AQUAE
GUAA_AQUAE
ID   GUAA_AQUAE              Reviewed;         510 AA.
AC   O66601;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
DE   AltName: Full=Glutamine amidotransferase;
GN   Name=guaA; OrderedLocusNames=aq_236;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.
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   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000657; AAC06558.1; -; Genomic_DNA.
DR   PIR; E70321; E70321.
DR   RefSeq; NP_213161.1; NC_000918.1.
DR   RefSeq; WP_010880099.1; NC_000918.1.
DR   AlphaFoldDB; O66601; -.
DR   SMR; O66601; -.
DR   STRING; 224324.aq_236; -.
DR   MEROPS; C26.957; -.
DR   PRIDE; O66601; -.
DR   EnsemblBacteria; AAC06558; AAC06558; aq_236.
DR   KEGG; aae:aq_236; -.
DR   PATRIC; fig|224324.8.peg.193; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_0; -.
DR   InParanoid; O66601; -.
DR   OMA; KRKIIGH; -.
DR   OrthoDB; 504464at2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000000798; 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   3: Inferred from homology;
KW   ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..510
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140088"
FT   DOMAIN          5..195
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          196..385
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000250"
FT   BINDING         223..229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   510 AA;  57858 MW;  2855029D68D1A667 CRC64;
     MQRRPILVVN FGSQYVQLIA RRVRELGVYS EIVHWDTPVE EIKKKNPYGI IFSGGPASVY
     AEGAPLPDKR IYELGVPILG ICYGLQVITH QLGGKVVRSE KQEYGRARLR IIKEDVIFEG
     IPKESDVWMS HADKVVELPE GFEVLAVSEN SPYAVIANRE KKIYGFQFHP EVTHTVFGKE
     MLANFIYGVC KAEKNWEMGD FIHEKIEEIR KTVGDAKVIA ALSGGVDSTV AAVLTHRAIG
     DKLHCFFIDH GLLRYKEREE VEKNLRSLGL PLTVVDASEE FLEKLKGVED PEEKRKIIGR
     TFIEVFEREA KKIEGAEFLL QGTLYPDVVE SAGIKGSAKI KTHHNVGGLP ERMNLKLLEP
     FRELFKDEVR KIGKLLGVPE EILRRHPFPG PGLAIRIIGE VNKKDLEILR KADYIFIQEL
     KKEGLYDRVW QAFAVLLPVK SVGVMGDVRT YEKVVALRAV ESVDGMTADW ARLPYDFLDR
     VMRRIINEVE GVNRVVYDIS SKPPSTIEWE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024