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Entry: A0A0V8HBN9_9BACI
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ID   A0A0V8HBN9_9BACI        Unreviewed;       424 AA.
AC   A0A0V8HBN9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Histidinol dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01024};
DE            Short=HDH {ECO:0000256|HAMAP-Rule:MF_01024};
DE            EC=1.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01024};
GN   Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024};
GN   ORFNames=GA0061094_3705 {ECO:0000313|EMBL:SCC28576.1};
OS   [Bacillus] enclensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=1402860 {ECO:0000313|EMBL:SCC28576.1, ECO:0000313|Proteomes:UP000181997};
RN   [1] {ECO:0000313|EMBL:SCC28576.1, ECO:0000313|Proteomes:UP000181997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SGD-1123 {ECO:0000313|EMBL:SCC28576.1,
RC   ECO:0000313|Proteomes:UP000181997};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC       histidinol to L-histidinaldehyde and then to L-histidine.
CC       {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_01024};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01024,
CC         ECO:0000256|PIRSR:PIRSR000099-4};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01024,
CC       ECO:0000256|PIRSR:PIRSR000099-4};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01024}.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010178, ECO:0000256|HAMAP-Rule:MF_01024,
CC       ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|RuleBase:RU004175}.
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DR   EMBL; FMAU01000005; SCC28576.1; -; Genomic_DNA.
DR   RefSeq; WP_058299621.1; NZ_KQ758486.1.
DR   AlphaFoldDB; A0A0V8HBN9; -.
DR   OrthoDB; 9805269at2; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000181997; Unassembled WGS sequence.
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   Gene3D; 1.20.5.1300; -; 1.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
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   NCBIfam; TIGR00069; hisD; 1.
DR   PANTHER; PTHR21256:SF2; HISTIDINE BIOSYNTHESIS TRIFUNCTIONAL PROTEIN; 1.
DR   PANTHER; PTHR21256; HISTIDINOL DEHYDROGENASE HDH; 1.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   PIRSF; PIRSF000099; Histidinol_dh; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01024};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01024};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01024}.
FT   ACT_SITE        319
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-1"
FT   ACT_SITE        320
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-1"
FT   BINDING         121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         183
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         206
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-2"
FT   BINDING         229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         251
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         254
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         407
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         412
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-4"
FT   BINDING         412
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
SQ   SEQUENCE   424 AA;  45664 MW;  181946593766A22A CRC64;
     MKIIKEVEEA SIKRSVDSGT EEQRKAVKKI IASVREKGDD SLKEYTEKFD GVTIEELKVS
     EVEIADAFAE MDTGMIKVIQ EAADNIRDFH EKQKQSSWFT TRPDGTMLGQ KLTPLDSVGV
     YVPGGTAAYP SSVLMNVLPA KVAGVGRITM VSPPGKDGKL SAGVLVAAKI AGVEEIYKVG
     GAQAVAALAY GTESISPVDK ITGPGNIFVA LAKREVFGDV DIDMIAGPSE IVVLADGSQH
     ADEIAADLLS QAEHDALASA VLVTTSEELA EEVSREVERQ LSTLPREEIA RRSINDYGAI
     YVTEDLEKAV DLVNNLAPEH LEILTADPFE TMAGIRHAGA IFLGRYSSEP VGDYFAGPNH
     VLPTNGTARF SSPLNVDEFM KKSSIISYSE KALRENGDKI AAFARLEGLE AHARAVEIRF
     NKRG
//
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