ID   HISXH_PELUB             Reviewed;         428 AA.
AC   Q4FMH0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   02-SEP-2026, entry version 114.
DE   RecName: Full=Histidinol dehydrogenase homolog {ECO:0000305};
DE            EC=1.1.-.- {ECO:0000305};
GN   OrderedLocusNames=SAR11_0801;
OS   Pelagibacter ubique (strain HTCC1062).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Candidatus Pelagibacterales; Candidatus Pelagibacteraceae;
OC   Candidatus Pelagibacter.
OX   NCBI_TaxID=335992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062;
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA   Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA   Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(2005).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P06988};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P06988};
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000084; AAZ21619.1; -; Genomic_DNA.
DR   RefSeq; WP_011281955.1; NC_007205.1.
DR   AlphaFoldDB; Q4FMH0; -.
DR   SMR; Q4FMH0; -.
DR   STRING; 335992.SAR11_0801; -.
DR   GeneID; 66295302; -.
DR   KEGG; pub:SAR11_0801; -.
DR   eggNOG; COG0141; Bacteria.
DR   HOGENOM; CLU_006732_3_3_5; -.
DR   OrthoDB; 9805269at2; -.
DR   Proteomes; UP000002528; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0000105; P:L-histidine biosynthetic process; IEA:InterPro.
DR   CDD; cd06572; Histidinol_dh; 1.
DR   FunFam; 3.40.50.1980:FF:000001; Histidinol dehydrogenase; 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; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..428
FT                   /note="Histidinol dehydrogenase homolog"
FT                   /id="PRO_0000135810"
FT   ACT_SITE        320
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   ACT_SITE        321
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         354
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         413
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
SQ   SEQUENCE   428 AA;  46658 MW;  0DE1C63534A76B41 CRC64;
     MAITYLKKSP KTSSTDDTKT TGIVQDLLKN IETTKEQGCI DLTKKFDKYD GEIIVSKERI
     EEIKKTLDQK TKDDVQFSYE RVRKFAEAQL KNYGQDFEVE LSDGLFAGQK LIPVNTAGCY
     VPGGRYAHIA SAVMSVTTAK VAGVKNVIAC SPPKEGVGAH PTIIYTADLC GADVILNLGG
     VPAIAAMTNG LFNNPPADII VGPGNQFVAE AKRILFGKVG IDLFAGPTEI GIIADAKADP
     EIVAVDLVGQ AEHGYNSPCW LYTTSKELAE KVMKRVPELI AELPEVPRTN ADAAWRDYGE
     VILCDTDEEM ATISDEYAPE HLEVQTENLE WFHKRLTNYG SLFIGEETTV AYGDKCSGTN
     HILPTKGAGR YTGGLFVGKF VKTLSFQRMT KESTELVGAA AARISRYEGM EAHARTGDVR
     LKKYGYSS
//