HSXH2_RHILO
ID HSXH2_RHILO Reviewed; 440 AA.
AC Q987C6;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Histidinol dehydrogenase homolog 2 {ECO:0000305};
DE EC=1.1.-.- {ECO:0000305};
GN OrderedLocusNames=mlr7107;
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}.
CC -!- CAUTION: The conserved zinc-binding site Asp residue in position 367 is
CC replaced by an Asn. {ECO:0000305}.
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DR EMBL; BA000012; BAB53277.1; -; Genomic_DNA.
DR RefSeq; WP_010914584.1; NC_002678.2.
DR AlphaFoldDB; Q987C6; -.
DR SMR; Q987C6; -.
DR STRING; 266835.14026681; -.
DR PRIDE; Q987C6; -.
DR EnsemblBacteria; BAB53277; BAB53277; BAB53277.
DR KEGG; mlo:mlr7107; -.
DR PATRIC; fig|266835.9.peg.5669; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_0_5; -.
DR OMA; FPSVTMM; -.
DR OrthoDB; 935289at2; -.
DR Proteomes; UP000000552; 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; Zinc.
FT CHAIN 1..440
FT /note="Histidinol dehydrogenase homolog 2"
FT /id="PRO_0000135831"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P06988"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P06988"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988"
SQ SEQUENCE 440 AA; 47089 MW; 76FF8FD9E42CA90C CRC64;
MSDVSFHDLS SLDATQRSSL LKRAEADLSV FVEKVRPIIQ AVKDEGDAAL IRFARELDKA
NVAEGGLQVS EAEFDAAFDK VEKDVVESIG FGIDNIRRFH EEQKPETMWL KEVRPGAYAG
DRYTPIASVA LYVPRGKGAF PSVTMMTSVP AVIAGVPQIA IVTPPTSDGS VDAATLVAAR
LAGVHTVYKC GGAQAVAAVA YGTETVKPAL KIVGPGSPWV VAAKSELSSI INTGLPAGPS
EAIIFADDSV DGGLAALDLL IEAEHGPDSS AYLVTHSRKV AEAALAALPQ HWSRMTEQRV
EFSRAVLTGK RGGIVLTASL EDSYRFINDY APEHLEILSK EPFAHLGHIT EAAEILMGPH
TPVTLANFVL GPNAVLPTSR WARTYGPLSV TDFVKRSSVG YVTSAAYPEL AKHARRLARY
EGFSSHENAV SEIRDRYLAG
