ID Q2IRX3_RHOP2 Unreviewed; 447 AA.
AC Q2IRX3;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Histidinol dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01024};
DE Short=HDH {ECO:0000256|HAMAP-Rule:MF_01024};
DE EC=1.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01024};
GN Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024};
GN OrderedLocusNames=RPB_4350 {ECO:0000313|EMBL:ABD09037.1};
OS Rhodopseudomonas palustris (strain HaA2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316058 {ECO:0000313|EMBL:ABD09037.1, ECO:0000313|Proteomes:UP000008809};
RN [1] {ECO:0000313|EMBL:ABD09037.1, ECO:0000313|Proteomes:UP000008809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HaA2 {ECO:0000313|EMBL:ABD09037.1,
RC ECO:0000313|Proteomes:UP000008809};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC histidinol to L-histidinaldehyde and then to L-histidine.
CC {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01024};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01024,
CC ECO:0000256|PIRSR:PIRSR000099-4};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01024,
CC ECO:0000256|PIRSR:PIRSR000099-4};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC {ECO:0000256|HAMAP-Rule:MF_01024}.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010178, ECO:0000256|HAMAP-Rule:MF_01024,
CC ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|RuleBase:RU004175}.
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DR EMBL; CP000250; ABD09037.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2IRX3; -.
DR STRING; 316058.RPB_4350; -.
DR KEGG; rpb:RPB_4350; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_3_5; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000008809; 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 Gene3D; 1.20.5.1300; -; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
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 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 Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024};
KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01024};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01024};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01024}.
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-1"
FT ACT_SITE 344
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-1"
FT BINDING 146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-2"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 431
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-4"
FT BINDING 436
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
SQ SEQUENCE 447 AA; 46637 MW; B55217EA4847F0C3 CRC64;
MSIRGLVGLC DSGSFQMPVR LDAASTDFPQ QFKAFLAMKR EVAADIEAAT RAIVDDVAAR
GDAALLDATA KFDRLTLDAA GLRVTAADID AAVQACDPDT VDALKFARDR IEFFHRRQLP
KDDRFTDALG VELGWRWSSI EAVGLYVPGG TAAYPSSVLM NAIPAKVAGV DRVVMVVPSP
DGKLNPLVLA AASLGGVTEI YRVGGAQAVA ALAYGTATIA PVSKIVGPGN AYVAAAKRQV
FGRVGIDMIA GPSEVVVVAD STGNPDWIAA DLLAQAEHDA NAQSILITDD AELADAVERA
VTAQLTTLPR AEIARASWEA YGAIIKVARL DDAVALADAI AAEHLEIITA DPEAFAAKIR
NAGAIFLGAH TPEAIGDYVG GSNHVLPTAR SARFSSGLGV LDFMKRTSIL KCGPEQLAAL
GPAAMTLGHA EGLEAHARSV GLRLNRR
//
