ID   HSXH1_RHILO             Reviewed;         500 AA.
AC   Q988P7;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Histidinol dehydrogenase homolog 1 {ECO:0000305};
DE            EC=1.1.-.- {ECO:0000305};
GN   OrderedLocusNames=mlr6649;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB52900.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q988P7; -.
DR   SMR; Q988P7; -.
DR   STRING; 266835.14026302; -.
DR   EnsemblBacteria; BAB52900; BAB52900; BAB52900.
DR   KEGG; mlo:mlr6649; -.
DR   eggNOG; COG0141; Bacteria.
DR   HOGENOM; CLU_006732_3_3_5; -.
DR   OMA; VCTPPDK; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd06572; Histidinol_dh; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR001692; Histidinol_DH_CS.
DR   InterPro; IPR012131; Hstdl_DH.
DR   PANTHER; PTHR21256; PTHR21256; 1.
DR   Pfam; PF00815; 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; Zinc.
FT   CHAIN           1..500
FT                   /note="Histidinol dehydrogenase homolog 1"
FT                   /id="PRO_0000135830"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        381
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   ACT_SITE        382
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         415
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
FT   BINDING         475
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P06988"
SQ   SEQUENCE   500 AA;  54015 MW;  71446C53BBF5D9F4 CRC64;
     MPPAGGIFHR PPTTRKSRRL TPRSACSNST CSRTWGEQPW LLALHSIDSD RNAGRRPCKR
     RAIAMIRTIK SARGSVVNGG NGAMTSAVQT LLDQVEQGGD RAVRELSIRF DKFDRDSYRL
     TKAEIDACIN SLTGREREDL DFAQDQIRNF AEAQRATLLD LEIETLPGVV LGHRNVPIQN
     VGCYVPGGKY PLLASAHMTV LTARVAGCER IITCAPPFQG KVAEKIVAAQ ALAGADEIYC
     LGGVQAIAAM AYGTETIAPV DMVAGPGNAY VAEAKRLLFG KVGIDLFAGP TETLVIADDS
     VDGELVATDL LGQAEHGVNS PAVLITNSEK LALDTVAEIG RLLTILPTAA IAAKAWEDFG
     EIILCETTKE MVAEADRLAS EHVQVMTRDP DHFLNSMRNY GALFLGARTN VSFGDKVIGT
     NHTLPTNKAA RYTGGLWVGK FLKTCTYQRI LTDEASALIG EYGSRLSLME GFVGHAEQSN
     IRVRRYGGRN VGYAMPVDPR