ID A0A0C1G2Z2_9FLAO Unreviewed; 378 AA.
AC A0A0C1G2Z2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=OA93_04870 {ECO:0000313|EMBL:KIA99502.1};
OS Flavobacterium sp. KMS.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1566023 {ECO:0000313|EMBL:KIA99502.1, ECO:0000313|Proteomes:UP000031466};
RN [1] {ECO:0000313|EMBL:KIA99502.1, ECO:0000313|Proteomes:UP000031466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:KIA99502.1,
RC ECO:0000313|Proteomes:UP000031466};
RA Smith A.K., Newman J.;
RT "Flavobacterium sp. KMS.";
RL Submitted (OCT-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIA99502.1}.
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DR EMBL; JSYP01000003; KIA99502.1; -; Genomic_DNA.
DR RefSeq; WP_039112018.1; NZ_JSYP01000003.1.
DR AlphaFoldDB; A0A0C1G2Z2; -.
DR STRING; 1566023.OA93_04870; -.
DR OrthoDB; 9790411at2; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000031466; 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};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01022, ECO:0000313|EMBL:KIA99502.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000031466}.
FT REGION 1..187
FT /note="Histidinol-phosphatase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT REGION 188..378
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 378 AA; 42989 MW; 74C1AEA994F4B486 CRC64;
MKKVLFIDRD GTMVLEPTDY QLDSFDKLEF YPKAFQYLAK IANELDYELV MVTNQDGLGT
DSHPEDSFWP IHNFIMKAFE NEGVTFEAVF IDKTFPHENA ITRKPRTGML TQYLDNPEYD
LENSFVLGDR LTDVELAKNL GSKAIFINTD EGLGSTEVAS KREELDPVIA LQTTDWKTIY
EFLKLEARSA SITRKTNETD IYINLNLDGT GKSKIETGIA FFDHMLDQIA RHGQMDLEIL
VKGDLEVDEH HTIEDTAIAL GEVFAKALGN KLGIERYGFC LPMDDCLSQV AIDFGGRNWL
VWETEFKREM VGKMPTEMFF HFFKSFSDGA KANINIKAEG TNEHHKIEAI FKAFAKAIKV
AVKRDTEKMI LPSTKGML
//
