HISX_PYRFU
ID HISX_PYRFU Reviewed; 375 AA.
AC O59626;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Histidinol dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.23;
GN Name=hisD; OrderedLocusNames=PF1659;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RA Kanai A., Oida H., Hasegawa A., Doi H.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC histidinol to L-histidinaldehyde and then to L-histidine.
CC {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AB013080; BAA25804.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81783.1; -; Genomic_DNA.
DR RefSeq; WP_011012805.1; NZ_CP023154.1.
DR AlphaFoldDB; O59626; -.
DR SMR; O59626; -.
DR STRING; 186497.PF1659; -.
DR EnsemblBacteria; AAL81783; AAL81783; PF1659.
DR GeneID; 41713487; -.
DR KEGG; pfu:PF1659; -.
DR PATRIC; fig|186497.12.peg.1725; -.
DR eggNOG; arCOG04352; Archaea.
DR HOGENOM; CLU_006732_3_3_2; -.
DR OMA; MVTGPGN; -.
DR OrthoDB; 55330at2157; -.
DR PhylomeDB; O59626; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000001013; Chromosome.
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; IPR012131; Hstdl_DH.
DR PANTHER; PTHR21256; PTHR21256; 1.
DR Pfam; PF00815; Histidinol_dh; 2.
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; Reference proteome; Zinc.
FT CHAIN 1..375
FT /note="Histidinol dehydrogenase"
FT /id="PRO_0000135903"
FT ACT_SITE 274
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 97
FT /note="G -> R (in Ref. 1; BAA25804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 42178 MW; F8874116A40B1A1B CRC64;
MDIEEYVREI LKDIRERGLE AIREYSKKFD GYEGPFEVSK EEFKEAEERI PERDKEIIKR
TLKRIEKYHR KQLKQDILYI ENGSLYGLIY KPLKRIGIYV PGGKPLPSTL MMVGVPARVA
GVKEIVVTNP PKDGKVNPYI LYIAKLLKIE EVYKLGGIQA IAAMAYGIGM KKVQKIFGPG
NKFVNEAKRQ VFGIVGIDSL AGPSEIAVIA DESADKDFVL YDLLSQLEHG KDSKAWLLTT
SKELADYCNR EGITVIVCSS LEECCKKANE IAPEHLEIIT REPLKLVDLI ENAGAIYLGL
YTPVPAADYF LGVNHVLPTG GAAKFMGVLT VWDFMKPISI AMVSREEFIS ERELGIRLAE
IEGIELHKKS LEVRK
