HISX_PICTO
ID HISX_PICTO Reviewed; 375 AA.
AC Q6KZD1;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=PTO1336;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT43921.1; -; Genomic_DNA.
DR RefSeq; WP_011178137.1; NC_005877.1.
DR AlphaFoldDB; Q6KZD1; -.
DR SMR; Q6KZD1; -.
DR STRING; 263820.PTO1336; -.
DR EnsemblBacteria; AAT43921; AAT43921; PTO1336.
DR GeneID; 2844768; -.
DR KEGG; pto:PTO1336; -.
DR PATRIC; fig|263820.9.peg.1387; -.
DR eggNOG; arCOG04352; Archaea.
DR HOGENOM; CLU_006732_3_3_2; -.
DR OMA; MVTGPGN; -.
DR OrthoDB; 55330at2157; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000000438; 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_0000135901"
FT ACT_SITE 274
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
SQ SEQUENCE 375 AA; 41836 MW; 5DA4E83583844BD1 CRC64;
MDIYEYVSNI ISDVRINGID ALKRYSEAFD NYSGGFTVTD DEIEDADKSI KPGEKDAIKN
IYERIYEYHK NQFEGQKINI KNGSIYGIIY RPIDRIGLYV PGKRALPSTL MMLGIPARIA
GVKSIVLCTA PENGNVNKYT LYIARLLGIR EIYKIGGVQA IAAMAYGISM KPVDKIFGPG
NKYVNEAKRQ VFGITGIDGL YGPSEICLIA DDSANINYIK NDLLSQLEHG EASSAYLITN
SLRIYNEVKL ENVKKYYKET VEESIELANE IAPEHLELLV NDPLKYLNII RNAGAVYMGE
YGPVPAGDYF LGVNHVLPTG SSARFSSVLT VYDFMKRISV AMPSKYDFLS AVDSGLKLAS
IENMKMHYKS MEARI
