HISX_PROM9
ID HISX_PROM9 Reviewed; 440 AA.
AC Q318Q4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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};
GN OrderedLocusNames=PMT9312_1581;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
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., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) 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: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; CP000111; ABB50641.1; -; Genomic_DNA.
DR AlphaFoldDB; Q318Q4; -.
DR SMR; Q318Q4; -.
DR STRING; 74546.PMT9312_1581; -.
DR EnsemblBacteria; ABB50641; ABB50641; PMT9312_1581.
DR KEGG; pmi:PMT9312_1581; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_3_3; -.
DR OMA; MVTGPGN; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000002715; 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; Zinc.
FT CHAIN 1..440
FT /note="Histidinol dehydrogenase"
FT /id="PRO_0000229861"
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 430
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
SQ SEQUENCE 440 AA; 48592 MW; 5D93F6C85EBF6D0F CRC64;
MGREPFNLKN LEMRIINNKK DAIQELKRIS SRTNSENNNK INLIVEEILQ EVKTYGDIAV
EKYTKKFDGF NPDPMQISED HLKDAWDEID SNLKRSLEVA HKRIKKFHEK EIPQSFTIKG
EHGDTVQRRW RPVKNAGIYI PGGRAAYPST VLMNAIPAKV AGVEEIIMVS PGNKEGEINK
TVLAAAHLSG IKKVFRIGGA QAIGALAFGT NQINKVDVIT GPGNIYVTTA KKLIYGSTGI
DSLAGPSEIL VIADETAQST HIASDLLAQA EHDPLASSIL LTTSKNQAKE VLEELYKKID
DHPRKEICMQ SIKNWGLIVI CENYELCIEL SNNFAPEHLE ILALDSKKIL EGIENAGAIF
LGKWTPEAVG DYLAGPNHTL PTSGNSRFSG SLGVETFMKN TSIIEFNEES LKVNSLDIIN
LAESEGLHSH ANSVKIRFED
