HISX_ZYMMO
ID HISX_ZYMMO Reviewed; 430 AA.
AC Q9RH05; Q5NM85;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Histidinol dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.23;
GN Name=hisD; Synonyms=hdh; OrderedLocusNames=ZMO1551;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Kang H.L., Kang H.S.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=19816441; DOI=10.1038/nbt1009-893;
RA Yang S., Pappas K.M., Hauser L.J., Land M.L., Chen G.L., Hurst G.B.,
RA Pan C., Kouvelis V.N., Typas M.A., Pelletier D.A., Klingeman D.M.,
RA Chang Y.J., Samatova N.F., Brown S.D.;
RT "Improved genome annotation for Zymomonas mobilis.";
RL Nat. Biotechnol. 27:893-894(2009).
CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC histidinol to L-histidinaldehyde and then to L-histidine.
CC {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF18281.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF088897; AAF18281.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE008692; AAV90175.2; -; Genomic_DNA.
DR RefSeq; WP_011241316.1; NZ_CP035711.1.
DR AlphaFoldDB; Q9RH05; -.
DR SMR; Q9RH05; -.
DR STRING; 264203.ZMO1551; -.
DR EnsemblBacteria; AAV90175; AAV90175; ZMO1551.
DR GeneID; 58027273; -.
DR KEGG; zmo:ZMO1551; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_3_5; -.
DR OMA; MVTGPGN; -.
DR OrthoDB; 935289at2; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000001173; 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..430
FT /note="Histidinol dehydrogenase"
FT /id="PRO_0000135889"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 328
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 406..430
FT /note="PAAVTLAKAEGLPAHAESVISRLNK -> LRL (in Ref. 1;
FT AAF18281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 46339 MW; 213A0D3F7609A6C4 CRC64;
MLLKLDSRKA DFQADFTRLV DERRESEGDV SRDVSAIIAD VKKRGDVAIA ELTQKFDRHD
LNKGGWQLTQ EEIKKACDSL PSELMDALKL AATRIRYCHE NQLPESSEMT DAAGVRMGVR
WQAVEAAGLY VPGGRAAYCS SVLMNAVPAK VAGVKRLVMV TPTPDGFVNP AVIAAAVISE
VDEIWKIGGA QAVAALALGT EKIKPVDVVV GPGNAWVAEA KRQLYGQVGI DMVAGPSEIV
VVADKDNDPE WLAADLLSQA EHDPTSQSIL ISDSEDLIEK TIEAVGRRLE KLETQKVARE
SWDKHGATIL VQSLDEAPAL VDRLAPEHLE LAVADPDALF ANVHHSGSVF LGRYTPEAIG
DYVGGPNHVL PTGRRARFSS GLSVIDFMKR TTYLNCSQEA LSKIGPAAVT LAKAEGLPAH
AESVISRLNK
