ID S6AFU9_PSERE Unreviewed; 437 AA.
AC S6AFU9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
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 ECO:0000313|EMBL:BAN46775.1};
GN ORFNames=PCA10_10430 {ECO:0000313|EMBL:BAN46775.1};
OS Pseudomonas resinovorans NBRC 106553.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN46775.1, ECO:0000313|Proteomes:UP000015503};
RN [1] {ECO:0000313|EMBL:BAN46775.1, ECO:0000313|Proteomes:UP000015503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN46775.1,
RC ECO:0000313|Proteomes:UP000015503};
RX PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA Fujita N., Nojiri H.;
RT "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT resinovorans Strain CA10 (NBRC 106553).";
RL Genome Announc. 1:e00488-13(2013).
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; AP013068; BAN46775.1; -; Genomic_DNA.
DR RefSeq; WP_016490977.1; NC_021499.1.
DR AlphaFoldDB; S6AFU9; -.
DR STRING; 1245471.PCA10_10430; -.
DR KEGG; pre:PCA10_10430; -.
DR PATRIC; fig|1245471.3.peg.1054; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_3_6; -.
DR OrthoDB; 9805269at2; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000015503; 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}; Reference proteome {ECO:0000313|Proteomes:UP000015503};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01024}.
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-1"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-1"
FT BINDING 136
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 197
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 220
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 243
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 265
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 265
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 268
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 268
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 367
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 367
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
FT BINDING 426
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 426
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01024,
FT ECO:0000256|PIRSR:PIRSR000099-3"
SQ SEQUENCE 437 AA; 46814 MW; EA4C4B5B8AD847B9 CRC64;
MTAPFAIRRL NAADPDFARH LDHLLSWESV SDDSVNQRVL DIIKAVRERG DAAVVEFTQR
FDGVQATSMA DLILPRERLE LALTRISSEQ REALETAAAR VRSYHEKQKQ DSWSYTEADG
TVLGQQVTPL DRAGLYVPGG KASYPSSVLM NAIPAKVAGV AEVVMVVPTP RGEINEIVLA
AACVAGVDRV FTIGGAQAVA ALAYGTESVP QVDKVVGPGN IYVATAKRHV FGQVGIDMIA
GPSEILVVCD GGTDPDWIAM DLFSQAEHDE DAQSILVSHD AAFLDKVAAS IDKLLPTMER
AEIIRTSLQN RGALILVADQ AQACQVANRI APEHLELSVA DPQAWLPQIR HAGAIFMGRY
TAEALGDYCA GPNHVLPTSG TARFSSPLGV YDFQKRSSII FCSADGASVL GKTASVLARG
ESLTAHARSA EYRIKGE
//
