ID   HISXH_RHIME             Reviewed;         456 AA.
AC   Q930I4;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Histidinol dehydrogenase homolog {ECO:0000305};
DE            EC=1.1.-.- {ECO:0000305};
GN   OrderedLocusNames=RA0212; ORFNames=SMa0398;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymA (megaplasmid 1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481432; DOI=10.1073/pnas.161294798;
RA   Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA   Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA   Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA   Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA   Long S.R.;
RT   "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT   meliloti pSymA megaplasmid.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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 381 is
CC       replaced by an Asn. {ECO:0000305}.
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DR   EMBL; AE006469; AAK64870.1; -; Genomic_DNA.
DR   PIR; D95288; D95288.
DR   RefSeq; NP_435458.3; NC_003037.1.
DR   RefSeq; WP_010967210.1; NC_003037.1.
DR   AlphaFoldDB; Q930I4; -.
DR   SMR; Q930I4; -.
DR   EnsemblBacteria; AAK64870; AAK64870; SMa0398.
DR   GeneID; 61599052; -.
DR   KEGG; sme:SMa0398; -.
DR   PATRIC; fig|266834.11.peg.220; -.
DR   HOGENOM; CLU_006732_3_0_5; -.
DR   OrthoDB; 9805269at2; -.
DR   Proteomes; UP000001976; Plasmid pSymA.
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; 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; Plasmid; Reference proteome; Zinc.
FT   CHAIN           1..456
FT                   /note="Histidinol dehydrogenase homolog"
FT                   /id="PRO_0000135833"
FT   ACT_SITE        347
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   ACT_SITE        348
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         279
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         440
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
SQ   SEQUENCE   456 AA;  48702 MW;  958D34D91C28DEEA CRC64;
     MTLRPQLARY KDKTMTSVSF YEYSKLNAEE KAALLRRSET DISGFIEKVA PILEAVRTEG
     DKALARFGRE LDKADVTEAN LKVTAAEFDA AFKLVDASVL ESVQFGIDNI RKFHEEQKPE
     AMWLKEIRPG AFAGDRFTPI QSVALYVPRG KGSFPSVTMM TSVPAVVAGV PNLAIVTPPA
     PDGSVDAATL VAARLAGVET VYKAGGAQAV AAVAYGTETV KPALKIVGPG SPWVVAAKRS
     LSGVIDTGLP AGPSEVMILA DDTVHGGLAA LDLLIEAEHG PDSSAYLVTH SGRVAEEALA
     ALPEHWARMT EQRTAFSKTV LSGKTGGIVL TSSIEESYEF VNAYAPEHLE LLSEQPFIHL
     GHITEASEIL MGTHTPVSIA NFSLGPNAVL PTSRWARTFG PLSVTDFVKR SSIGYVTAPA
     YPEFARHSHN LAIYEGFSSH ALAVSPVRDA YLKKGA
//