HISX_BIFLO
ID HISX_BIFLO Reviewed; 471 AA.
AC Q8G4S9;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Histidinol dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01024};
DE Short=HDH {ECO:0000255|HAMAP-Rule:MF_01024};
DE EC=1.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01024};
GN Name=hisD {ECO:0000255|HAMAP-Rule:MF_01024}; OrderedLocusNames=BL1295;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC histidinol to L-histidinaldehyde and then to L-histidine.
CC {ECO:0000255|HAMAP-Rule:MF_01024}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01024};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01024};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01024};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC {ECO:0000255|HAMAP-Rule:MF_01024}.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01024}.
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DR EMBL; AE014295; AAN25096.1; -; Genomic_DNA.
DR RefSeq; NP_696460.1; NC_004307.2.
DR AlphaFoldDB; Q8G4S9; -.
DR SMR; Q8G4S9; -.
DR STRING; 206672.BL1295; -.
DR EnsemblBacteria; AAN25096; AAN25096; BL1295.
DR KEGG; blo:BL1295; -.
DR PATRIC; fig|206672.9.peg.144; -.
DR HOGENOM; CLU_006732_3_1_11; -.
DR OMA; MVTGPGN; -.
DR PhylomeDB; Q8G4S9; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000000439; Chromosome.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06572; Histidinol_dh; 1.
DR HAMAP; MF_01024; HisD; 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 Amino-acid biosynthesis; Histidine biosynthesis; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..471
FT /note="Histidinol dehydrogenase"
FT /id="PRO_0000135733"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT ACT_SITE 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 236
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 443
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
SQ SEQUENCE 471 AA; 50257 MW; 36D6D724978BDC88 CRC64;
MLRWGVMSEN IMRIIDLRGQ NLSRAELLAA MPRAAMGTSE ATDLVRPILD DVKERGAAAL
RDFEEKFDHV RPKNLRVPVE AIKDALTTLD PEVRAAIEES VRRARAVAAN QVPKDFYTDL
AEGARVAERW IPIQRVGLYV PGGKAVYPSS VIMNAVPAQA AGVESLAIAT PPARDNEEGL
PNKTILATCA ILGVDEVYAV GGAQAIAMFA YGAKGSEPQD GDILCDPVDK ITGPGNIFVA
TAKSLVSAFV GIDAVAGPTE IGIIADETAN PSLLAADLIG QAEHDELAGS VLFTDSTEIA
DKVQESLKYR VPRTEHAERV HTSLSGTQSA IVLTDGLDQS IDAANAYAAE HLEIQTKDAD
AVVKRIKNAG AIFRGPYSPV PLGDYMSGSN HVLPTGGTAR FAAGLGVHTF MKPVEVIEYD
EEGLKALAAR INAFAVSEDL PAHGECVLSR FVKDPYDKAT LREQEKEAGL R
