HISXH_CERS4
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 03-AUG-2022, entry version 89.
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; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; 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 12203
RC / 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 OMA; FPSVTMM; -.
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 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..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
