HISXH_COLP3
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 03-AUG-2022, entry version 104.
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; Proteobacteria; 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 EnsemblBacteria; AAZ25938; AAZ25938; CPS_2061.
DR KEGG; cps:CPS_2061; -.
DR HOGENOM; CLU_006732_3_0_6; -.
DR OMA; FPSVTMM; -.
DR OrthoDB; 935289at2; -.
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 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 Metal-binding; Oxidoreductase; Reference proteome; 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
