HIS7_BACTN
ID HIS7_BACTN Reviewed; 374 AA.
AC Q8ABA7;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
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, ECO:0000303|PubMed:25848029};
DE EC=3.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:25848029};
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=BT_0203;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2]
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=25848029; DOI=10.1073/pnas.1423570112;
RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L.,
RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D.,
RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., Dunaway-Mariano D.,
RA Allen K.N., Farelli J.D.;
RT "Panoramic view of a superfamily of phosphatases through substrate
RT profiling.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015).
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 ECO:0000269|PubMed:25848029};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01022,
CC ECO:0000269|PubMed:25848029};
CC Note=Binds 2 Mg(2+) ions. {ECO:0000250|UniProtKB:Q9S5G5};
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; AE015928; AAO75310.1; -; Genomic_DNA.
DR RefSeq; NP_809116.1; NC_004663.1.
DR RefSeq; WP_008766230.1; NC_004663.1.
DR AlphaFoldDB; Q8ABA7; -.
DR SMR; Q8ABA7; -.
DR STRING; 226186.BT_0203; -.
DR PaxDb; Q8ABA7; -.
DR PRIDE; Q8ABA7; -.
DR DNASU; 1075538; -.
DR EnsemblBacteria; AAO75310; AAO75310; BT_0203.
DR GeneID; 60926167; -.
DR KEGG; bth:BT_0203; -.
DR PATRIC; fig|226186.12.peg.201; -.
DR eggNOG; COG0131; Bacteria.
DR HOGENOM; CLU_044308_0_0_10; -.
DR InParanoid; Q8ABA7; -.
DR OMA; PEDTFWP; -.
DR UniPathway; UPA00031; UER00011.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000001414; 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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Hydrolase;
KW Lyase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Reference proteome.
FT CHAIN 1..374
FT /note="Histidine biosynthesis bifunctional protein HisB"
FT /id="PRO_0000158200"
FT REGION 1..183
FT /note="Histidinol-phosphatase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
FT REGION 184..374
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 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022"
SQ SEQUENCE 374 AA; 42432 MW; 7824A7FBE5A3EAD2 CRC64;
MKKKILFIDR DGTLVIEPPI DYQLDSLEKL EFYPRVFRNL GFIRSKLDFE FVMVTNQDGL
GTSSFPEDTF WPAHNLMLKT LAGEGITFDD ILIDRSFPED NAPTRKPRTG MLTKYIDNPE
YDLAESFVIG DRPTDVELAK NLGCRAIYLQ EATDDLKEKG LEEVCALATT DWDQVAEFLF
AGERKAEVRR TTKETDIYVS LNLDGNGGCD ISTGLGFFDH MLEQIGKHSG MDLTIRVKGD
LEVDEHHTIE DTAIALGECI YQALGSKRGI ERYGYALPMD DCLCQVCLDF GGRPWLVWDA
EFNREKIGEM PTEMFLHFFK SLSDAAKMNL NIKAEGQNEH HKIEGIFKAL ARALKMALKR
DIYHFELPSS KGVL
