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GUAA_NEIG2
ID   GUAA_NEIG2              Reviewed;         521 AA.
AC   B4RJH7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=NGK_2643;
OS   Neisseria gonorrhoeae (strain NCCP11945).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=521006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCCP11945;
RX   PubMed=18586945; DOI=10.1128/jb.00566-08;
RA   Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT   "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL   J. Bacteriol. 190:6035-6036(2008).
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; CP001050; ACF31242.1; -; Genomic_DNA.
DR   RefSeq; WP_003702177.1; NC_011035.1.
DR   PDB; 5TW7; X-ray; 2.35 A; A/B/C/D/E/F=1-521.
DR   PDBsum; 5TW7; -.
DR   AlphaFoldDB; B4RJH7; -.
DR   SMR; B4RJH7; -.
DR   MEROPS; C26.957; -.
DR   EnsemblBacteria; ACF31242; ACF31242; NGK_2643.
DR   KEGG; ngk:NGK_2643; -.
DR   HOGENOM; CLU_014340_0_5_4; -.
DR   OMA; KRKIIGH; -.
DR   OrthoDB; 504464at2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000002564; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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.
FT   CHAIN           1..521
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_1000120341"
FT   DOMAIN          5..197
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   DOMAIN          198..390
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   BINDING         225..231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   STRAND          5..10
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           16..25
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          29..34
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           39..45
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          48..52
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           68..72
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           82..90
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          103..110
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   TURN            114..118
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          126..132
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          134..139
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          145..150
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          153..160
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   TURN            161..164
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          165..170
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           180..189
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           200..215
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          220..224
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           228..241
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           242..244
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          245..251
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           259..271
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          274..279
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           281..288
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           294..315
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          321..323
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           328..331
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          361..363
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   TURN            365..368
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           371..381
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           385..388
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           397..400
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           408..427
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           436..439
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          441..454
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          461..473
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          479..481
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   HELIX           486..499
FT                   /evidence="ECO:0007829|PDB:5TW7"
FT   STRAND          503..509
FT                   /evidence="ECO:0007829|PDB:5TW7"
SQ   SEQUENCE   521 AA;  57656 MW;  208D32100AA27D2D CRC64;
     MTQDKILILD FGSQVTRLIA RRVREAHVYC ELHSFDMPLD EIKAFNPKGI ILSGGPNSVY
     ESDYQADTGI FDLGIPVLGI CYGMQFMAHH LGGEVQPGNQ REFGYAQVKT IDSGLTRGIQ
     DDAPNTLDVW MSHGDKVSKL PDGFAVIGDT PSCPIAMMEN TEKQFYGIQF HPEVTHTKQG
     RALLNRFVLD ICGAQPGWTM PNYIEEAVAK IREQVGSDEV ILGLSGGVDS SVAAALIHRA
     IGDQLTCVFV DHGLLRLNEG KMVMDMFARN LGVKVIHVDA EGQFMAKLAG VTDPEKKRKI
     IGAEFIEVFD AEEKKLTNAK WLAQGTIYPD VIESAGAKTK KAHAIKSHHN VGGLPENMKL
     KLLEPLRDLF KDEVRELGVA LGLPREMVYR HPFPGPGLGV RILGEVKKEY ADLLRQADDI
     FIQELRNTTD ENGTSWYDLT SQAFAVFLPV KSVGVMGDGR TYDYVVALRA VITSDFMTAH
     WAELPYSLLG RVSNRIINEV KGINRVVYDV SGKPPATIEW E
 
 
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