ID K6Y1L8_9ALTE Unreviewed; 356 AA.
AC K6Y1L8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
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:GAC17786.1};
GN ORFNames=GARC_0805 {ECO:0000313|EMBL:GAC17786.1};
OS Paraglaciecola arctica BSs20135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC17786.1, ECO:0000313|Proteomes:UP000006327};
RN [1] {ECO:0000313|EMBL:GAC17786.1, ECO:0000313|Proteomes:UP000006327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSs20135 {ECO:0000313|EMBL:GAC17786.1,
RC ECO:0000313|Proteomes:UP000006327};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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 -!- 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}.
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:GAC17786.1}.
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DR EMBL; BAEO01000010; GAC17786.1; -; Genomic_DNA.
DR RefSeq; WP_007616922.1; NZ_BAEO01000010.1.
DR AlphaFoldDB; K6Y1L8; -.
DR STRING; 493475.GARC_0805; -.
DR eggNOG; COG0131; Bacteria.
DR eggNOG; COG0241; Bacteria.
DR OrthoDB; 9790411at2; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000006327; 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; 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.
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:UP000006327};
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; 39660 MW; C83D561209AEDAB5 CRC64;
MSQQPLLFID RDGTLVEEPA IDKQLDSLEK LVFEPQVLPV LLKLQQNGFR LIMVSNQDGL
GTDSFPQADF DLAHNKMMDI FTSQGVTFDD VLICPHFDSD NCTCRKPKLG LVKDYLQQGK
VDFTRSFVIG DRDTDMQLAE NMGIVGIKYN RETNNWQNIE KQLLASSRVA TVVRKTSETN
INVTVDLDST AKSTIETGLG FFDHMLDQIA THGGFELNLT VDGDLHIDDH HSVEDTALAL
GEAIKKALGD KRGIGRFGFA LPMDECRAEC IMDISNRPHL KFDAEFSRDQ VGEMATEMVP
HFFYSIAQAM GLSLHLSTTE GNAHHQVESL FKVFGRALRQ AIHKQGEALP SSKGTL
//
