ID   HISXH_COLP3             Reviewed;         446 AA.
AC   Q483H8;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Histidinol dehydrogenase homolog {ECO:0000305};
DE            EC=1.1.-.- {ECO:0000305};
GN   OrderedLocusNames=CPS_2061;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P06988};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P06988};
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The conserved zinc-binding site Asp residue in position 368 is
CC       replaced by an Asn. {ECO:0000305}.
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DR   EMBL; CP000083; AAZ25938.1; -; Genomic_DNA.
DR   RefSeq; WP_011042883.1; NC_003910.7.
DR   AlphaFoldDB; Q483H8; -.
DR   SMR; Q483H8; -.
DR   STRING; 167879.CPS_2061; -.
DR   KEGG; cps:CPS_2061; -.
DR   HOGENOM; CLU_006732_3_0_6; -.
DR   Proteomes; UP000000547; Chromosome.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:InterPro.
DR   CDD; cd06572; Histidinol_dh; 1.
DR   Gene3D; 1.20.5.1300; -; 1.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
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   NCBIfam; TIGR00069; hisD; 1.
DR   PANTHER; PTHR21256:SF2; HISTIDINE BIOSYNTHESIS TRIFUNCTIONAL PROTEIN; 1.
DR   PANTHER; PTHR21256; HISTIDINOL DEHYDROGENASE HDH; 1.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   PIRSF; PIRSF000099; Histidinol_dh; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Oxidoreductase; Zinc.
FT   CHAIN           1..446
FT                   /note="Histidinol dehydrogenase homolog"
FT                   /id="PRO_0000135758"
FT   ACT_SITE        334
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   ACT_SITE        335
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         427
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
SQ   SEQUENCE   446 AA;  48236 MW;  4B8C883BF8A096FA CRC64;
     MTHKVKIHRL SDLSAEQRNK LLQRTESNLD NFIDIVKPII ENVKLNGDKA LSEYAKKFDK
     AEVSTDQIQV TQAEFDEAFT LVDEEVIQTL SYSIDNIKKF HEAQMPEEMW MKQIRPGCYA
     GDRFTPINAV ACYIPRGKGS FPSVAIMTAV PAIVAGVPTA IIITPPGTDG KVDAATLVVA
     KLVGIDKVFK CGGAQGIAAV AYGTNTVPKC DKVVGPGSPF VVAAKKLLAD IIHPGTPAGP
     SEAIVLADDT ANPKLAALDL LVEAEHGPDS SAFLVTNSKE LAEQAQVAIN EYWQHMDRLR
     VDFSSTVLSG DNGGIVLTST FEEAVDFCND YAAEHLLILS KSPFDHLGKI INAGEILLGE
     NTPISIANYT LGPNAVLPTS MAAKTASPLS VFDYLKSCSI GYLTREGYEE LAPHTYRFAK
     YEGFDAHANA VSHLRDEAIK SEKKIK
//