HIS7_PECAS
ID HIS7_PECAS Reviewed; 355 AA.
AC Q6D409;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=ECA2585;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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 ---------------------------------------------------------------------------
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; BX950851; CAG75484.1; -; Genomic_DNA.
DR RefSeq; WP_011094130.1; NC_004547.2.
DR AlphaFoldDB; Q6D409; -.
DR SMR; Q6D409; -.
DR STRING; 218491.ECA2585; -.
DR EnsemblBacteria; CAG75484; CAG75484; ECA2585.
DR KEGG; eca:ECA2585; -.
DR PATRIC; fig|218491.5.peg.2619; -.
DR eggNOG; COG0131; Bacteria.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_044308_0_0_6; -.
DR OMA; PEDTFWP; -.
DR OrthoDB; 1278103at2; -.
DR UniPathway; UPA00031; UER00011.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000007966; 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;
KW Reference proteome; Zinc.
FT CHAIN 1..355
FT /note="Histidine biosynthesis bifunctional protein HisB"
FT /id="PRO_0000158209"
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; 39764 MW; EA5110C3F374E066 CRC64;
MGQKYLFIDR DGTLIAEPPE DFQVDRLDKL ALEPDVIPSL LALQKAGYTL VMITNQDGLG
TDSFPQETFD PPHNLMMQIL TSQGIHFEHV LICPHLPADN CTCRKPKTEL VTAYLNGGLM
DVANSYVIGD RQTDIQLAQN MGITGLLYQR GGLNWQAITD QLTKRNRHAH VNRVTRETAI
DVNVWLDQEG GSKINTGVGF FDHMLDQIAT HGGFRMNIEV KGDLYIDDHH TVEDTGLALG
EALNNALGDK RGIGRFGFIL PMDECLARCA LDISGRPHLE YKAEFNYQRV GDLSTEMVEH
FFRSLSYSMA CTLHLKTKGR NDHHRVESLF KVFGRTLRQA IRVEGDTLPS SKGVL
