ID A0A1Y6KS99_9GAMM Unreviewed; 356 AA.
AC A0A1Y6KS99;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 ECO:0000313|EMBL:SMY15060.1};
GN ORFNames=PAQU9191_00276 {ECO:0000313|EMBL:SMY15060.1};
OS Photobacterium aquimaris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=512643 {ECO:0000313|EMBL:SMY15060.1, ECO:0000313|Proteomes:UP000196485};
RN [1] {ECO:0000313|Proteomes:UP000196485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=type strain: CECT 9192 {ECO:0000313|Proteomes:UP000196485};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (JUN-2017) 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|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01022};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
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}.
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DR EMBL; FYAH01000001; SMY15060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6KS99; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000196485; 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; cd07503; HAD_HisB-N; 1.
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; IPR013954; PNK3P.
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; PF00475; IGPD; 1.
DR Pfam; PF08645; PNK3P; 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}; Reference proteome {ECO:0000313|Proteomes:UP000196485};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01022}.
FT REGION 1..167
FT /note="Histidinol-phosphatase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT REGION 168..356
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT ACT_SITE 12
FT /note="Proton donor"
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 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
SQ SEQUENCE 356 AA; 39574 MW; D3FFA1E6DACA40C7 CRC64;
MSKEKILFID RDGTLIVEPP VDFQVDRLDK LKFEPNVIPA LLALQNAGYK LVMVTNQDGL
GTNSYPQADF DAPHTMMMDI FDSQGVHFSD VLICPHFDHQ QCSCRKPKLG LVKDYLQQGR
VDFATSAVIG DRQTDLQLAE NMAIRGIQYH PQTMNWQQIV TDLTTQPRLA EVIRTTKETD
IRVKVNLDQT GGNTISTGLG FFDHMLDQIA THGGFQMTLT VDGDLHIDDH HSVEDAALAL
GEALRQALGD KRGIGRFGFS LPMDECLAQC ALDLSGRPYL KFDATFSRDQ VGDLSTEMVP
HFFRSLTDTL ACTLHLSSTG NNDHHIVESL FKAFGRTLRQ AIKVEGNELP SSKGVL
//
