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HISX_PROMA
ID   HISX_PROMA              Reviewed;         440 AA.
AC   Q7VA26;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, 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=Pro_1643;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAQ00687.1; -; Genomic_DNA.
DR   RefSeq; NP_876034.1; NC_005042.1.
DR   RefSeq; WP_011125793.1; NC_005042.1.
DR   AlphaFoldDB; Q7VA26; -.
DR   SMR; Q7VA26; -.
DR   STRING; 167539.Pro_1643; -.
DR   EnsemblBacteria; AAQ00687; AAQ00687; Pro_1643.
DR   GeneID; 54200967; -.
DR   KEGG; pma:Pro_1643; -.
DR   PATRIC; fig|167539.5.peg.1738; -.
DR   eggNOG; COG0141; Bacteria.
DR   HOGENOM; CLU_006732_3_3_3; -.
DR   OMA; MVTGPGN; -.
DR   OrthoDB; 935289at2; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000001420; 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..440
FT                   /note="Histidinol dehydrogenase"
FT                   /id="PRO_0000135813"
FT   ACT_SITE        332
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   ACT_SITE        333
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         134
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         196
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         219
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         267
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         366
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         420
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         425
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT   BINDING         425
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
SQ   SEQUENCE   440 AA;  47721 MW;  B7150E41CA0679AF CRC64;
     MSERKQILNC IDDPQQALIM LKRISARTSL EVQENAISSV QNILTEVKQL GDEALFRLTE
     KFDGFIPKPL EITPEQTLEA WEKTPTPLQE ALQLAKNRIE AFHKYQIPKD FLKEGIHGEL
     LGKNWSPVEK AGIYIPGGRA AYPSTVLMNA VPALVAGVNE IIMVSPAGPN GQLNRTVLAA
     AYIAGIKKIF RIGGAQAIGA LSYGTQTIPR VDVISGPGNL YVTLAKKLVY GQVGIDSLAG
     PSEVLIIADH SADVEQVATD LLAQAEHDPL AASILLTTES NLAKKINLEI ENQLKDHPRS
     AICRKSLKDW GLIVICKDIK SCAALSNSFA PEHLELLIEK PFEFISQIKN AGAIFLGEWS
     PEATGDYLAG PNHTLPTSGT ARFSSALSVE TFMKSTSIIN FNQAALNKTS AAIMELANSE
     GLHSHSRSIE IRRSKPSSDD
 
 
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