ID A0A0M4L472_9GAMM Unreviewed; 436 AA.
AC A0A0M4L472;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Histidinol dehydrogenase {ECO:0000313|EMBL:ALE01200.1};
DE EC=1.1.1.23 {ECO:0000313|EMBL:ALE01200.1};
GN ORFNames=W908_00390 {ECO:0000313|EMBL:ALE01200.1};
OS Candidatus Pseudothioglobus singularis PS1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Pseudothioglobus.
OX NCBI_TaxID=1125411 {ECO:0000313|EMBL:ALE01200.1, ECO:0000313|Proteomes:UP000068905};
RN [1] {ECO:0000313|EMBL:ALE01200.1, ECO:0000313|Proteomes:UP000068905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PS1 {ECO:0000313|EMBL:ALE01200.1,
RC ECO:0000313|Proteomes:UP000068905};
RX PubMed=26494659;
RA Marshall K.T., Morris R.M.;
RT "Genome Sequence of 'Candidatus Thioglobus singularis' Strain PS1, a
RT Mixotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL Genome Announc. 3:e01155-e01115(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000099-4};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000099-4};
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|RuleBase:RU004175}.
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DR EMBL; CP006911; ALE01200.1; -; Genomic_DNA.
DR RefSeq; WP_020026423.1; NZ_CP006911.1.
DR AlphaFoldDB; A0A0M4L472; -.
DR STRING; 1125411.W908_00390; -.
DR KEGG; tsn:W908_00390; -.
DR PATRIC; fig|1125411.7.peg.77; -.
DR OrthoDB; 9805269at2; -.
DR Proteomes; UP000068905; Chromosome.
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:SF14; HISTIDINOL DEHYDROGENASE; 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 ECO:0000256|PIRSR:PIRSR000099-4}; NAD {ECO:0000256|PIRSR:PIRSR000099-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000099};
KW Reference proteome {ECO:0000313|Proteomes:UP000068905};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR000099-4}.
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT ACT_SITE 320
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-1"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 408
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 413
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000099-3"
SQ SEQUENCE 436 AA; 47182 MW; 09014D26C408187B CRC64;
MAIKYLKKGK TAADKAIDDA EVSEVVKNTL KVIEEKGDSA VREFSEKFDN YSPKSYKLSS
AEIDGLIANV SDRDMKDIKF AQEQVRNFAQ AQRDSMQDIE VETMPGVILG HKNIPVQSVG
CYVPAGKFPM VASAHMSVVT ASVAKVPRIV ACTPPYQGAP NAAVIAAMHL GGAHEIYVIG
GIQAVGAMAL GTESINPVDM LVGPGNAFVA EAKRQLFGRV GIDLFAGPTE TMVIADETVD
AELCATDLLG QAEHGYNSPA VLVTNSQKLA EETQVEIDRI LTILPTADTA GVSWAEYGEV
VVCDTYDEML EVANDIASEH VQVMTDRDDW FLDHMHSYGA LFLGPRTNVS NGDKVIGTNH
TLPTKKAGRY TGGLWVGKYL KTHSYQKITT DEAAVKIGRY CSRLCMLESF VGHAEQANIR
VRRYGGEDVP YGKAAQ
//
