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HIS7_XANC5
ID   HIS7_XANC5              Reviewed;         375 AA.
AC   Q3BUF5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=XCV1877;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10;
RX   PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
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   -!- 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}.
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DR   EMBL; AM039952; CAJ23554.1; -; Genomic_DNA.
DR   RefSeq; WP_011347187.1; NZ_CP017190.1.
DR   AlphaFoldDB; Q3BUF5; -.
DR   SMR; Q3BUF5; -.
DR   STRING; 456327.BJD11_13040; -.
DR   EnsemblBacteria; CAJ23554; CAJ23554; XCV1877.
DR   KEGG; xcv:XCV1877; -.
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; UP000007069; 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.
FT   CHAIN           1..375
FT                   /note="Histidine biosynthesis bifunctional protein HisB"
FT                   /id="PRO_1000063450"
FT   REGION          1..168
FT                   /note="Histidinol-phosphatase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   REGION          169..375
FT                   /note="Imidazoleglycerol-phosphate dehydratase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   ACT_SITE        10
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
SQ   SEQUENCE   375 AA;  41993 MW;  3B8FC9F1BAB1D28E CRC64;
     MTPILFVDRD GTLITEPADY QIDAYEKLRF VDHVIPAMLK LRDAGYQFVI VSNQDGLGSE
     SYPRASFEGP NNLMLQIFAS QGIEFRDVLI DCSWPADNAP TRKPGIGLMV PYLQDRSIDW
     ARSAMVGDRI TDIQFAHNLN IRGFQLRTDE FGGEWDWPGI AHELADAPRR AVVQRNTKET
     RIRVELDLDR VAEPKTATGL PFFDHMLEQI GKHGGFALEI RAEGDLHIDE HHTIEDTGLA
     LGQALREALG NKRGIGRYGF DPESSPWRVA GDKAQHGFTL PMDETIASAA LDFSGRPYFV
     FDGEFKRERV GDMPTELVPH FFRSICDASG LNLHLTVRGE NDHHKVEACF KALARALRQA
     IRREGTALPT TKGAL
 
 
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