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HIS7_ECOL6
ID   HIS7_ECOL6              Reviewed;         355 AA.
AC   Q8FG50;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Histidine biosynthesis bifunctional protein HisB {ECO:0000255|HAMAP-Rule:MF_01022};
DE   Includes:
DE     RecName: Full=Histidinol-phosphatase {ECO:0000255|HAMAP-Rule:MF_01022};
DE              EC=3.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01022};
DE   Includes:
DE     RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_01022};
DE              Short=IGPD {ECO:0000255|HAMAP-Rule:MF_01022};
DE              EC=4.2.1.19 {ECO:0000255|HAMAP-Rule:MF_01022};
GN   Name=hisB {ECO:0000255|HAMAP-Rule:MF_01022}; OrderedLocusNames=c2549;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-
CC         4-yl)-2-oxopropyl phosphate + H2O; Xref=Rhea:RHEA:11040,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57766, ChEBI:CHEBI:58278; EC=4.2.1.19;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01022};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-histidinol phosphate = L-histidinol + phosphate;
CC         Xref=Rhea:RHEA:14465, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57699, ChEBI:CHEBI:57980; EC=3.1.3.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01022};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01022};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01022};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the histidinol-
CC       phosphatase family. {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       imidazoleglycerol-phosphate dehydratase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01022}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN81004.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN81004.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000080122.1; NC_004431.1.
DR   AlphaFoldDB; Q8FG50; -.
DR   SMR; Q8FG50; -.
DR   STRING; 199310.c2549; -.
DR   EnsemblBacteria; AAN81004; AAN81004; c2549.
DR   KEGG; ecc:c2549; -.
DR   eggNOG; COG0131; Bacteria.
DR   eggNOG; COG0241; Bacteria.
DR   HOGENOM; CLU_044308_0_0_6; -.
DR   OMA; PEDTFWP; -.
DR   UniPathway; UPA00031; UER00011.
DR   UniPathway; UPA00031; UER00013.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07914; IGPD; 1.
DR   Gene3D; 3.30.230.40; -; 2.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_01022; Bifunc_HisB; 1.
DR   HAMAP; MF_00076; HisB; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR020566; His_synth_bifunc_HisB.
DR   InterPro; IPR005954; HisB_N.
DR   InterPro; IPR006543; Histidinol-phos.
DR   InterPro; IPR038494; IGPD_sf.
DR   InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
DR   InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR23133; PTHR23133; 1.
DR   Pfam; PF00475; IGPD; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR   TIGRFAMs; TIGR01261; hisB_Nterm; 1.
DR   TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
DR   PROSITE; PS00954; IGP_DEHYDRATASE_1; 1.
DR   PROSITE; PS00955; IGP_DEHYDRATASE_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Hydrolase;
KW   Lyase; Magnesium; Metal-binding; Multifunctional enzyme; Zinc.
FT   CHAIN           1..355
FT                   /note="Histidine biosynthesis bifunctional protein HisB"
FT                   /id="PRO_0000158207"
FT   REGION          1..166
FT                   /note="Histidinol-phosphatase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   REGION          167..355
FT                   /note="Imidazoleglycerol-phosphate dehydratase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   ACT_SITE        11
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
SQ   SEQUENCE   355 AA;  40303 MW;  616CDFC19EFCF806 CRC64;
     MSQKYLFIDR DGTLISEPPS DFQVDRFDKL AFEPGVIPEL LRLQKAGYKL VMITNQDGLG
     TQSFPQADFD GPHNLMMQIF TSQGVQFDEV LICPHLPADE CDCRKPKVKL VERYLAEQAM
     DRANSYVIGD RATDIQLAEN MGINGLRYDR EILNWPMIGE QLTKRDRYAH VVRNTKETQI
     DVQVWLDREG GSKINTGVGF FDHMLDQIAT HGGFRMEINV KGDLYIDDHH TVEDTGLALG
     EALKIALGDK RGICRFGFVL PMDECLARCA LDISGRPHLE YKAEFTYQRV GDLSTEMIEH
     FFRSLSYTMG VTLHLKTKGK NDHHRVESLF KAFGRTLRQA IRVEGDTLPS SKGVL
 
 
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