HISXH_ALKCK
ID HISXH_ALKCK Reviewed; 424 AA.
AC Q5WIU9;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Histidinol dehydrogenase homolog {ECO:0000305};
DE EC=1.1.-.- {ECO:0000305};
GN OrderedLocusNames=ABC1168;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AP006627; BAD63706.1; -; Genomic_DNA.
DR RefSeq; WP_011246020.1; NC_006582.1.
DR AlphaFoldDB; Q5WIU9; -.
DR SMR; Q5WIU9; -.
DR STRING; 66692.ABC1168; -.
DR EnsemblBacteria; BAD63706; BAD63706; ABC1168.
DR KEGG; bcl:ABC1168; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_3_9; -.
DR OMA; VCTPPDK; -.
DR OrthoDB; 935289at2; -.
DR Proteomes; UP000001168; 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..424
FT /note="Histidinol dehydrogenase homolog"
FT /id="PRO_0000135724"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P06988"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P06988"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988"
SQ SEQUENCE 424 AA; 46122 MW; 6131743AA063022E CRC64;
MAQYIKQGKS ESELKDSHGK VEQTVASLIA RIEKEGETAV RELSRQFDNW DPEQFRLSAE
EIEKIVRSVP DQVKADICFA QEQIRHFAEQ QRASIQDIEV ETRPGVFLGH KNIPVNSVGC
YIPGGRYPMV ASSHMSILTA KVAGVKRVIG CTPPINGEIP AATVTAMHFA GADEIYILGG
VQAMTAMAVG TETIEAVDML VGPGNAFVAE AKRQLFGRVG IDLFAGPTEV LIIADDTADG
EMVATDLLGQ AEHGPTSPAA LITTSKKLAE ETVAEIERQL QTLPTADVAK VAWEEHGMII
LVDDLAEAVV EADKLAYEHV QVLTENPNYF LDHMTNYGAL FLGPETNVAY GDKVIGTNHT
LPTKKAAKYT GGLWVGKFLK NCTYQRCTPE ASAEIGRIAE RLCELEGFIG HKAQASLRVK
RYGK
