ID A0A0G1DGG0_9BACT Unreviewed; 429 AA.
AC A0A0G1DGG0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Histidinol dehydrogenase, histidinol dehydrogenase {ECO:0000313|EMBL:KKS96652.1};
DE EC=1.1.1.23 {ECO:0000313|EMBL:KKS96652.1};
GN ORFNames=UV73_C0009G0003 {ECO:0000313|EMBL:KKS96652.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWA2_43_14.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618443 {ECO:0000313|EMBL:KKS96652.1, ECO:0000313|Proteomes:UP000034894};
RN [1] {ECO:0000313|EMBL:KKS96652.1, ECO:0000313|Proteomes:UP000034894}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010178, ECO:0000256|PIRNR:PIRNR000099,
CC ECO:0000256|RuleBase:RU004175}.
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:KKS96652.1}.
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DR EMBL; LCFP01000009; KKS96652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1DGG0; -.
DR STRING; 1618443.UV73_C0009G0003; -.
DR PATRIC; fig|1618443.3.peg.1164; -.
DR Proteomes; UP000034894; Unassembled WGS sequence.
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:InterPro.
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 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000099}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT ACT_SITE 328
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
SQ SEQUENCE 429 AA; 46766 MW; 9F432EE03E26B555 CRC64;
MKVVKLKELS SKDYQRIAAR SSGTNPHILP KVRQIMEAVR KEGDKYLVGE FKRRFGKSNF
KSFLVSKDEI REAYRQVDKR LITGLKQMIK NITMVHKAHL PKKTDRKVFS EKGIAVWRVW
RAIEIVGIYI PGGKAIYPSS VLMTAIPAAI AGCREIVMCS PARGDGQIPP ATLVAADMVG
LTKIFKTGGV EAIAAMTYGT ETIPAVYKIF GAGNSLVTAA KLLALEKIAI DMPAGPSEIF
IIADKEANPG FIAADLLADG EHGFDSACIL LTTSRKVAEE TIKEIKKQLL KLSTGKMAEA
SIRKFGLFAV VDSLEEAIDF TNSYAPEHLE IMVENPEKVV ANITNAGSVF LGEYTSKSAG
DYATGANHVL PTGGMAKNYP PLGVEAFGKW MQVQKCSRKG LSGIRETIRI LAEYEGLPAH
DVSADIRFK
//
