HIS7_SALTY
ID HIS7_SALTY Reviewed; 355 AA.
AC P10368;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
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=STM2074;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=3062174; DOI=10.1016/0022-2836(88)90194-5;
RA Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.;
RT "Structure and function of the Salmonella typhimurium and Escherichia coli
RT K-12 histidine operons.";
RL J. Mol. Biol. 203:585-606(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RC STRAIN=LT2;
RA Barnes W.M., Husson R.N., Whittier R.;
RL Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases.
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=CAA31825.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X13464; CAA31825.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006468; AAL20978.1; -; Genomic_DNA.
DR EMBL; J01804; AAA88617.1; -; Genomic_DNA.
DR PIR; JS0159; DWEBHB.
DR RefSeq; NP_461019.1; NC_003197.2.
DR RefSeq; WP_000080044.1; NC_003197.2.
DR AlphaFoldDB; P10368; -.
DR SMR; P10368; -.
DR STRING; 99287.STM2074; -.
DR PaxDb; P10368; -.
DR EnsemblBacteria; AAL20978; AAL20978; STM2074.
DR GeneID; 1253595; -.
DR KEGG; stm:STM2074; -.
DR PATRIC; fig|99287.12.peg.2196; -.
DR HOGENOM; CLU_044308_0_0_6; -.
DR OMA; PEDTFWP; -.
DR PhylomeDB; P10368; -.
DR BioCyc; SENT99287:STM2074-MON; -.
DR UniPathway; UPA00031; UER00011.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000001014; 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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
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_0000158220"
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"
FT CONFLICT 7
FT /note="F -> L (in Ref. 1; CAA31825)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="C -> S (in Ref. 1; CAA31825)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="N -> S (in Ref. 1; CAA31825)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="G -> R (in Ref. 1; CAA31825)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="G -> R (in Ref. 1; CAA31825)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="Missing (in Ref. 1; CAA31825)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="D -> N (in Ref. 1; CAA31825)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="L -> V (in Ref. 1; CAA31825)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 40183 MW; 8E732AFCA49A32A3 CRC64;
MSQKYLFIDR DGTLISEPPS DFQVDRFDKL AFEPEVIPVL LKLQKAGFKL VMITNQDGLG
TQSFPQADFD GPHNLMMQIF TSQGVCFDEV LICPHLPADD CDCRKPKVKL VERYLAEQAM
DSANSYVIGD RATDIQLADN MGITGLRYHR ETLNWTMIGE QLTKRDRYAH VVRNTKETQI
DVSVWLDREG NSKINTGVGF FDHMLDQIAT HGGFRMEITV KGDLYIDDHH TVEDTGLALG
EALKLALGDK RGICRFGFVL PMDECLARCA LDISGRPHLE YKAEFTYQRV GDLSTEMIEH
FFRSLSYTMG VTLHLKTKGK NDHHRVESLF KAFGRTLRQA IRVEGDTLPS SKGVL
