HISX_BUCMH
ID HISX_BUCMH Reviewed; 201 AA.
AC Q9RQ82;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Histidinol dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.23;
DE Flags: Fragment;
GN Name=hisD;
OS Buchnera aphidicola subsp. Melaphis rhois.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=118103;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10555290; DOI=10.1093/oxfordjournals.molbev.a026071;
RA Clark M.A., Moran N.A., Baumann P.;
RT "Sequence evolution in bacterial endosymbionts having extreme base
RT compositions.";
RL Mol. Biol. Evol. 16:1586-1598(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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF129283; AAF13776.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RQ82; -.
DR SMR; Q9RQ82; -.
DR PRIDE; Q9RQ82; -.
DR UniPathway; UPA00031; UER00014.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-EC.
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:UniProtKB-UniPathway.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR012131; Hstdl_DH.
DR PANTHER; PTHR21256; PTHR21256; 1.
DR Pfam; PF00815; Histidinol_dh; 1.
DR PRINTS; PR00083; HOLDHDRGNASE.
DR SUPFAM; SSF53720; SSF53720; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Histidine biosynthesis; Metal-binding; NAD;
KW Oxidoreductase; Zinc.
FT CHAIN 1..>201
FT /note="Histidinol dehydrogenase"
FT /id="PRO_0000135745"
FT NON_TER 201
SQ SEQUENCE 201 AA; 22028 MW; E0FA5769CF7DB395 CRC64;
MKNCLKIIHW DRCSIEEREK ILSRPILDDL SAIKKQVKTI ISDVNSLGDQ ALYNYTNIFD
KIKLNNIKIS HQDLVKAELC IDVKAKNAIQ VAIDNIRTFH ISQNISTLNI EINKGIYCQQ
IVRPIGSVGL YIPGGSAPLL STVLMLAIPA RIAGCKKIVL CSPPPITNEV LYASKICGVQ
EIFQVGGAQA IAALGFGTET I