HISX_AZOBR
ID HISX_AZOBR Reviewed; 128 AA.
AC P18786;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Putative histidinol dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.23;
DE Flags: Fragment;
GN Name=hisD;
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sp6;
RX PubMed=2664449; DOI=10.1007/bf00334360;
RA Fani R., Bazzicalupo M., Damiani G., Bianchi A., Schipani C.,
RA Sgaramella V., Polsinelli M.;
RT "Cloning of histidine genes of Azospirillum brasilense: organization of the
RT ABFH gene cluster and nucleotide sequence of the hisB gene.";
RL Mol. Gen. Genet. 216:224-229(1989).
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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000305}.
CC -!- CAUTION: Highly divergent compared to other bacterial HisD.
CC {ECO:0000305}.
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DR EMBL; X17435; CAA35477.1; -; Genomic_DNA.
DR PIR; PE0006; PE0006.
DR AlphaFoldDB; P18786; -.
DR UniPathway; UPA00031; UER00014.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Histidine biosynthesis; NAD; Oxidoreductase.
FT CHAIN <1..128
FT /note="Putative histidinol dehydrogenase"
FT /id="PRO_0000135719"
FT REGION 21..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 128 AA; 14111 MW; BDF52031D2B04CCD CRC64;
ILVQTAPAGP IDVLIGRPAL QRPDIAPRHH APPHRAEREA VEADRSRRTA GDGWGFAGLR
QLPAHAGGQH QQGREGQEKA SGRRHVRCHI PLCALSVHTT MHTHALSGIA TDGHRRFRRR
HLCRPRAS