HISXH_PELUB
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 03-AUG-2022, entry version 100.
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; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC Pelagibacteraceae; 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 EnsemblBacteria; AAZ21619; AAZ21619; SAR11_0801.
DR GeneID; 66295302; -.
DR KEGG; pub:SAR11_0801; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_3_5; -.
DR OMA; MKIVTWQ; -.
DR OrthoDB; 935289at2; -.
DR Proteomes; UP000002528; Chromosome.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:InterPro.
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 InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR001692; Histidinol_DH_CS.
DR InterPro; IPR022695; Histidinol_DH_monofunct.
DR InterPro; IPR012131; Hstdl_DH.
DR PANTHER; PTHR21256; PTHR21256; 1.
DR Pfam; PF00815; Histidinol_dh; 1.
DR PIRSF; PIRSF000099; Histidinol_dh; 1.
DR PRINTS; PR00083; HOLDHDRGNASE.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR00069; hisD; 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
