ID A0A0M1JEF4_9GAMM Unreviewed; 353 AA.
AC A0A0M1JEF4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE SubName: Full=Histidinol dehydrogenase {ECO:0000313|EMBL:KOR31698.1};
DE Flags: Fragment;
GN ORFNames=TI05_11945 {ECO:0000313|EMBL:KOR31698.1};
OS Achromatium sp. WMS3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Achromatium.
OX NCBI_TaxID=1604836 {ECO:0000313|EMBL:KOR31698.1, ECO:0000313|Proteomes:UP000036918};
RN [1] {ECO:0000313|EMBL:KOR31698.1, ECO:0000313|Proteomes:UP000036918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS3 {ECO:0000313|EMBL:KOR31698.1};
RX PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT "Metabolic diversity and ecological niches of Achromatium populations
RT revealed with single-cell genomic sequencing.";
RL Front. Microbiol. 6:822-822(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|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:KOR31698.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JXSO01000290; KOR31698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M1JEF4; -.
DR PATRIC; fig|1604836.3.peg.2056; -.
DR Proteomes; UP000036918; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000036918};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KOR31698.1"
SQ SEQUENCE 353 AA; 37381 MW; 9C2458059A09D20D CRC64;
QALANLAAPE RTALNHAAQR IYAYAERQRL ESWSYTDSDG TLLGQQITPL ESVGIYVPGG
KAAYPSSVLM NAIPATVAGV PELIMVTPTP QGYSNELVLA AASLAGVTKV FAIGGAQAIA
ALAYGTATIP RVDKIVGPGN SYVAAAKQAV FGQVGIDMLA GPSEILIICD GATHPDWIAM
DLFSQAEHDE DAQAILISLD LDYIHQVQNS IERLLPTMER HQIIATALQT RGACILVKDL
AEACTIANHI APEHLELSVA DPQSLLKDIR HAGAIFMGQY TAEALGDYCA GPNHVLPTSR
TARFSSPLGV YDFQKRTSLI MATSTSAKIL GKTATCLATS EGLTAHARSA EYR
//
