HISX_VIBVU
ID HISX_VIBVU Reviewed; 431 AA.
AC Q8D8Q0;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Histidinol dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01024};
DE Short=HDH {ECO:0000255|HAMAP-Rule:MF_01024};
DE EC=1.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01024};
GN Name=hisD {ECO:0000255|HAMAP-Rule:MF_01024}; OrderedLocusNames=VV1_2919;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC histidinol to L-histidinaldehyde and then to L-histidine.
CC {ECO:0000255|HAMAP-Rule:MF_01024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH;
CC Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699,
CC ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01024};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01024};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01024};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC {ECO:0000255|HAMAP-Rule:MF_01024}.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01024}.
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DR EMBL; AE016795; AAO11252.1; -; Genomic_DNA.
DR RefSeq; WP_011080739.1; NC_004459.3.
DR AlphaFoldDB; Q8D8Q0; -.
DR SMR; Q8D8Q0; -.
DR EnsemblBacteria; AAO11252; AAO11252; VV1_2919.
DR KEGG; vvu:VV1_2919; -.
DR HOGENOM; CLU_006732_3_0_6; -.
DR OMA; MVTGPGN; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000002275; Chromosome 1.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06572; Histidinol_dh; 1.
DR HAMAP; MF_01024; HisD; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR001692; Histidinol_DH_CS.
DR InterPro; IPR022695; Histidinol_DH_monofunct.
DR InterPro; IPR012131; Hstdl_DH.
DR PANTHER; PTHR21256; PTHR21256; 1.
DR Pfam; PF00815; Histidinol_dh; 1.
DR PIRSF; PIRSF000099; Histidinol_dh; 1.
DR PRINTS; PR00083; HOLDHDRGNASE.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR00069; hisD; 1.
DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Histidine biosynthesis; Metal-binding; NAD;
KW Oxidoreductase; Zinc.
FT CHAIN 1..431
FT /note="Histidinol dehydrogenase"
FT /id="PRO_0000135877"
FT ACT_SITE 323
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT ACT_SITE 324
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 411
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
SQ SEQUENCE 431 AA; 46039 MW; D026BAA67F9D813E CRC64;
MRTVVWQSLS ETQQDAILER PAITEGANIT AAVAEVIAKV RAEGDAALFE LTEKFDRVKP
ESIRVTEQEI EEASARLTAK MKQALEQAYA NIAKFHNAQK PTPIKVETQP GVVCEQVTRP
IQKVGLYIPG GSAPLPSTVL MLGVPAQIAG CRKVVLCSPP PIADEILYVA KLCNIDEVYN
VGGGQAVAAM AYGTESVTKV DKIFGPGNAY VTEAKRQVSN DFRGAAIDMP AGPSEVLVIA
DETADADFIA ADLLSQAEHG PDSQVVLVTP SVLIADQVTD AVQKQLKQLS RASIAEKALA
SSLIIIADSL TQAVSISNYY GPEHLIVQTK NPRELLPLLD NAGSIFLGDW SPESAGDYAS
GTNHVLPTYG YTRTYSSLGL ADFSKRMTIQ ELSAEGLKTL APTVVTMAEA EGLDAHKRAV
TIRVEKLNAR G
