ID A0A0D7W2F6_9FLAO Unreviewed; 381 AA.
AC A0A0D7W2F6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=PK35_07880 {ECO:0000313|EMBL:KJD32888.1};
OS Tamlana nanhaiensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tamlana.
OX NCBI_TaxID=1382798 {ECO:0000313|EMBL:KJD32888.1, ECO:0000313|Proteomes:UP000032361};
RN [1] {ECO:0000313|EMBL:KJD32888.1, ECO:0000313|Proteomes:UP000032361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FHC16 {ECO:0000313|EMBL:KJD32888.1,
RC ECO:0000313|Proteomes:UP000032361};
RX PubMed=25735434; DOI=10.1007/s10482-015-0410-x;
RA Liu X., Lai Q., Du Y., Li G., Sun F., Shao Z.;
RT "Tamlana nanhaiensis sp. nov., isolated from surface seawater collected
RT from the South China Sea.";
RL Antonie Van Leeuwenhoek 107:1189-1196(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: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 -!- 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:KJD32888.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JTDV01000005; KJD32888.1; -; Genomic_DNA.
DR RefSeq; WP_044626161.1; NZ_JTDV01000005.1.
DR AlphaFoldDB; A0A0D7W2F6; -.
DR STRING; 1382798.PK35_07880; -.
DR PATRIC; fig|1382798.3.peg.2919; -.
DR OrthoDB; 9790411at2; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000032361; 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; 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; 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:KJD32888.1};
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:UP000032361}.
FT REGION 1..190
FT /note="Histidinol-phosphatase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT REGION 191..381
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 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
SQ SEQUENCE 381 AA; 43439 MW; 580BE5376069FDE6 CRC64;
MSKTKVLFID RDGTLVLEPP VDYQLDSLEK LEFYPKVFQY MAKIASELDF ELVMVTNQDG
LGTDSFPEDT FWPAQNKIID AFKKEGVTFT AIHIDKTFPH ENAETRKPRT GLLTQYFDKE
KYDLENSFVL GDRITDMELA KNLGAKGIYL SEDPELGADE IESSKQDILD CIALTSTDWK
EIYEFLKLKD RVSEITRNTN ETQIYIKLNL DGSGKNDIDT GLSFFDHMLD QIGRHGAMDL
TIKVNGDLEV DEHHTIEDTM IALGELFHKA LGNKLGIERY GFCLPMDDCL AQVAVDFGGR
NWLEWDAEFK REKIGDMPTE MFYHLFKSFT DGAKCNLNVK AEGVNEHHKI EGIFKAFAKA
MKMAVKRDAN KMFLPSTKGM L
//
