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Entry: A0A0N0KZK4_9MICO
LinkDB: A0A0N0KZK4_9MICO
Original site: A0A0N0KZK4_9MICO 
ID   A0A0N0KZK4_9MICO        Unreviewed;       436 AA.
AC   A0A0N0KZK4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Histidinol dehydrogenase {ECO:0000256|ARBA:ARBA00016531, ECO:0000256|HAMAP-Rule:MF_01024};
DE            Short=HDH {ECO:0000256|HAMAP-Rule:MF_01024};
DE            EC=1.1.1.23 {ECO:0000256|ARBA:ARBA00012965, ECO:0000256|HAMAP-Rule:MF_01024};
GN   Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024};
GN   ORFNames=AEQ27_08230 {ECO:0000313|EMBL:KPG84311.1};
OS   Frigoribacterium sp. RIT-PI-h.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frigoribacterium.
OX   NCBI_TaxID=1690245 {ECO:0000313|EMBL:KPG84311.1, ECO:0000313|Proteomes:UP000037934};
RN   [1] {ECO:0000313|Proteomes:UP000037934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIT-PI-h {ECO:0000313|Proteomes:UP000037934};
RA   Tran P.N., Lee Y.P., Gan H.M., Savka M.A.;
RT   "Whole genome sequencing of endophytes isolated from poison ivy
RT   (Toxicodendron radicans).";
RL   Submitted (JUL-2015) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001654, 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|ARBA:ARBA00004940, 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01024}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPG84311.1}.
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DR   EMBL; LHOZ01000065; KPG84311.1; -; Genomic_DNA.
DR   RefSeq; WP_054146164.1; NZ_LHOZ01000065.1.
DR   AlphaFoldDB; A0A0N0KZK4; -.
DR   PATRIC; fig|1690245.3.peg.242; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000037934; 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; 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.
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|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRSR:PIRSR000099-4};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01024};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01024}; Reference proteome {ECO:0000313|Proteomes:UP000037934};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-4}.
FT   ACT_SITE        332
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-1"
FT   ACT_SITE        333
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-1"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         263
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         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         266
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         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         366
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         366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         420
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
FT   BINDING         425
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         425
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT                   ECO:0000256|PIRSR:PIRSR000099-3"
SQ   SEQUENCE   436 AA;  44971 MW;  B8946EB393AD3E21 CRC64;
     MIQTTDLRGL APTHAQLLDL VPRSHADVGA ATDAARRLVD DVRERGAAAL RDQAARFDGV
     RPDTLRVATQ TIDDAVAALD PLVKEALVES IARVTQASRA QVPASTTTRP APGAVIEQRW
     QPVTRAGVYV PGGKAVYPSS VVMNVVPAQV AGVSSIALVS PAQREHGGGV HPVILGAAGL
     LGIDEVYAIG GAGAIGALAY GVPELELEPV QVITGPGNNF VAAAKQLVRG RVGIDSVAGA
     TEILVIADDS ADATLVAVDL ISQAEHDEEA SAVLVTDSAA FGEAVVAELT RLVPRTLSAA
     RVRTALSGRQ SAVVLVDDLR QAAAFSNAYG PEHLEVQTRD DDAVLADVTD AGAIFVGPDT
     PVSLGDYLAG SNHVLPTSGQ SRFSSGLGAF TFLRPQQIVR YDAEALGVVA ERLVALSNAE
     LLPAHGEAVA ARLSRP
//
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