ID A0A1H6T3X7_9BACT Unreviewed; 374 AA.
AC A0A1H6T3X7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Histidine biosynthesis bifunctional protein HisB {ECO:0000256|HAMAP-Rule:MF_01022};
DE Includes:
DE RecName: Full=Histidinol-phosphatase {ECO:0000256|HAMAP-Rule:MF_01022};
DE EC=3.1.3.15 {ECO:0000256|HAMAP-Rule:MF_01022};
DE Includes:
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000256|HAMAP-Rule:MF_01022};
DE Short=IGPD {ECO:0000256|HAMAP-Rule:MF_01022};
DE EC=4.2.1.19 {ECO:0000256|HAMAP-Rule:MF_01022};
GN Name=hisB {ECO:0000256|HAMAP-Rule:MF_01022};
GN ORFNames=SAMN05216327_103368 {ECO:0000313|EMBL:SEI70980.1};
OS Dyadobacter sp. SG02.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1855291 {ECO:0000313|EMBL:SEI70980.1, ECO:0000313|Proteomes:UP000199631};
RN [1] {ECO:0000313|EMBL:SEI70980.1, ECO:0000313|Proteomes:UP000199631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG02 {ECO:0000313|EMBL:SEI70980.1,
RC ECO:0000313|Proteomes:UP000199631};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_01022};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|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:0000256|ARBA:ARBA00005047, ECO:0000256|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:0000256|HAMAP-Rule:MF_01022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01022}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC imidazoleglycerol-phosphate dehydratase family. {ECO:0000256|HAMAP-
CC Rule:MF_01022}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the histidinol-
CC phosphatase family. {ECO:0000256|HAMAP-Rule:MF_01022}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01022}.
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DR EMBL; FNYL01000003; SEI70980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6T3X7; -.
DR STRING; 1855291.SAMN05216327_103368; -.
DR OrthoDB; 9790411at2; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000199631; Unassembled WGS sequence.
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; 3.40.50.1000; HAD superfamily/HAD-like; 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_Su5_D2-typ_SF.
DR NCBIfam; TIGR01662; HAD-SF-IIIA; 1.
DR NCBIfam; TIGR01261; hisB_Nterm; 1.
DR NCBIfam; TIGR01656; Histidinol-ppas; 1.
DR PANTHER; PTHR23133:SF2; IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE; 1.
DR PANTHER; PTHR23133; IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE HIS7; 1.
DR Pfam; PF13242; Hydrolase_like; 1.
DR Pfam; PF00475; IGPD; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
DR PROSITE; PS00954; IGP_DEHYDRATASE_1; 1.
DR PROSITE; PS00955; IGP_DEHYDRATASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01022};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01022};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW Rule:MF_01022}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01022};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01022};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01022};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01022};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01022}.
FT REGION 1..182
FT /note="Histidinol-phosphatase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT REGION 183..374
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT ACT_SITE 10
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
SQ SEQUENCE 374 AA; 42361 MW; FA081806D7AF4D34 CRC64;
MKKVLFIDRD GTIIVEPPTD FQVDSLEKLE FLPKAISALR KIAEETDYEL VMVTNQDGLG
TNSFPEDTFW PAQNKMVKTL EGEDIHFADV HIDRSFPEDN LPTRKPGIGM LTAYFSHEYD
LANSYVIGDR LTDVQLAVNL GAKAILFRPE LPEEGITDQM NQSTALVTSD WDAIYEHLKL
PSRKAFVERN TKETQIKVEL NLDGSGRSDI HTGLGFFDHM LDQLARHSGA DLSIHVEGDL
HIDEHHTIED TALALGEAYR QAIGDKRGIS RYGFLLPMDE ALAQVAIDFS GRPWIVWDAE
FKREKIGEMP TEMFFHFFKS FSDTSLSNLN IKVEGDNEHH KIESIFKAFA KAIKMAVKRD
LKALDFMPST KEVL
//
