HISX_RHOPA
ID HISX_RHOPA Reviewed; 431 AA.
AC P60861;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Histidinol dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01024};
DE Short=HDH {ECO:0000255|HAMAP-Rule:MF_01024};
DE EC=1.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01024};
GN Name=hisD {ECO:0000255|HAMAP-Rule:MF_01024}; OrderedLocusNames=RPA4531;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC histidinol to L-histidinaldehyde and then to L-histidine.
CC {ECO:0000255|HAMAP-Rule:MF_01024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH;
CC Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699,
CC ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01024};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01024};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01024};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC {ECO:0000255|HAMAP-Rule:MF_01024}.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01024}.
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DR EMBL; BX572607; CAE29971.1; -; Genomic_DNA.
DR RefSeq; WP_011160063.1; NC_005296.1.
DR AlphaFoldDB; P60861; -.
DR SMR; P60861; -.
DR STRING; 258594.RPA4531; -.
DR PRIDE; P60861; -.
DR EnsemblBacteria; CAE29971; CAE29971; RPA4531.
DR GeneID; 66895681; -.
DR KEGG; rpa:RPA4531; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_3_5; -.
DR OMA; MVTGPGN; -.
DR PhylomeDB; P60861; -.
DR BioCyc; RPAL258594:TX73_RS23160-MON; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000001426; Chromosome.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06572; Histidinol_dh; 1.
DR HAMAP; MF_01024; HisD; 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 Amino-acid biosynthesis; Histidine biosynthesis; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..431
FT /note="Histidinol dehydrogenase"
FT /id="PRO_0000135835"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT ACT_SITE 328
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
SQ SEQUENCE 431 AA; 45117 MW; E560EA9B918F015B CRC64;
MPLRLDNASP DFASKFKAFL AMKREVAADI EAATRAIVDD VAHRGDAALL EATEKFDRLT
LDAAGMRVGE AEVEAAVKAC DSETVDALKL ARDRIEFFHR RQLPKDDRFT DPLGVELGWR
WSAIEAVGLY VPGGTAAYPS SVLMNAIPAK VAGVERVVMV VPSPGGTLNP LVLAAAQLAG
ATEIYRIGGA QAVAALAYGT ATIAPVAKIV GPGNAYVAAA KRLVFGRVGI DMIAGPSEVV
VVADKTANPD WIAADLLAQA EHDANAQSIL ITDSAVLAAD VERALAAQLT TLPRVKIARA
SWDEFGAIIK VAKLEDAVPL ANAIAAEHLE IMTADPEAFA DKIRNAGAIF LGGHTPEAIG
DYVGGSNHVL PTARSARFSS GLGVLDFMKR TSILKCGPEQ LAVLGPAAMA LGKAEGLDAH
ARSVGLRLNQ R
