ID   HISXH_CERS4             Reviewed;         441 AA.
AC   Q3J4H6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Histidinol dehydrogenase homolog {ECO:0000305};
DE            EC=1.1.-.- {ECO:0000305};
GN   OrderedLocusNames=RHOS4_07400; ORFNames=RSP_2155;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC
RC   12203 / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The conserved zinc-binding site Asp residue in position 368 is
CC       replaced by an Asn. {ECO:0000305}.
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DR   EMBL; CP000143; ABA78308.1; -; Genomic_DNA.
DR   RefSeq; WP_011337274.1; NZ_CP030271.1.
DR   RefSeq; YP_352209.1; NC_007493.2.
DR   AlphaFoldDB; Q3J4H6; -.
DR   SMR; Q3J4H6; -.
DR   STRING; 272943.RSP_2155; -.
DR   EnsemblBacteria; ABA78308; ABA78308; RSP_2155.
DR   KEGG; rsp:RSP_2155; -.
DR   PATRIC; fig|272943.9.peg.1051; -.
DR   eggNOG; COG0141; Bacteria.
DR   OrthoDB; 9805269at2; -.
DR   PhylomeDB; Q3J4H6; -.
DR   Proteomes; UP000002703; Chromosome 1.
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   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; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..441
FT                   /note="Histidinol dehydrogenase homolog"
FT                   /id="PRO_0000229864"
FT   ACT_SITE        334
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   ACT_SITE        335
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         427
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
SQ   SEQUENCE   441 AA;  46882 MW;  B1481F195AAEA18E CRC64;
     MVQVNFQVLA ELDAAGRAAL LRRSETDLSM FLEKVGPILE AVRTEGDAAL VRFGRELDRA
     EGLTREGLKV TEAEFDEAFG LVEPEIVAAI RFAIGNIRTF HEEQAPEPMW LKELRPGAFA
     GDRFTPIRSV ALYVPRGKGS FPSVTMMTSV PAVVAKVPQI AIFTPPAPDG RVDAATLVAA
     RLAGVETVYK VGGAQAVAAA AYGTETVTPA LKIVGPGSPW VVAAKRLLAG VIDPGLPAGP
     SESIILADET VHGGLAALDL LIEAEHGPDS SAWLVTHSRQ VAEEALAALP GHWSAMTPQR
     VDFSQAVLCG RAGGIVLTGS AEESHAFVND YAPEHLQILS EKPFEHLGRI TEAAEVLMGP
     HTPITIANFC LGPNAVLPTS RGARTWGPLS VHDFLRRSSV GYVTAPAYPE LAEVAKRLAE
     YEGFSSHANA VGPMRDAYLK R
//