HISX_MYCPA
ID HISX_MYCPA Reviewed; 480 AA.
AC P60860;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=MAP_1293;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS03610.1; -; Genomic_DNA.
DR AlphaFoldDB; P60860; -.
DR SMR; P60860; -.
DR STRING; 262316.MAP_1293; -.
DR EnsemblBacteria; AAS03610; AAS03610; MAP_1293.
DR KEGG; mpa:MAP_1293; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_1_11; -.
DR OMA; MVTGPGN; -.
DR UniPathway; UPA00031; UER00014.
DR Proteomes; UP000000580; 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..480
FT /note="Histidinol dehydrogenase"
FT /id="PRO_0000135797"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 216
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 411
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 470
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
FT BINDING 470
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01024"
SQ SEQUENCE 480 AA; 49373 MW; D51BE3BAB2ABB107 CRC64;
MYRPDIDLSS SGTMDTVSPT PASPMAGIDL RGAELTAARL RSALPRGGAD VETVLPKVRP
IVQAVAERGA DAALEFGASF DGVRPAAVRV PEAALDKALA DLDAAVADAL RVMIDRARAV
HADQRRTDVT TTLGPGATVT ERWVPVERVG LYVPGGNAVY PSSVVMNVVP AQAAGVASLV
VASPPQAQFD GLPHPTILAA ARLLGVDEVW AVGGAQAVAL LAYGGTDTGA EWPGFSSDRA
RSASSPGADA ELVPVDMITG PGNIYVTAAK RLCRSRVGID AEAGPTEIAI LADHTADPAH
VAADLISQAE HDEMAGSVLV TPSEDLAAAT DAELAAQLPT TVHRERVTAA LGGRQSAIIL
VDDLDAGITV VNAYAAEHLE IQTADAAAVA GRIRAAGAVF VGPYSPVSLG DYCAGSNHVL
PTAGSARHSS GLSVQTFLRG IHVVDYTEAA LKDVSGHVIT LAQAEDLPAH GEAIRRRFER
