ADHC_MYCTO
ID ADHC_MYCTO Reviewed; 346 AA.
AC P9WQC4; L0TE62; P0A4X0; P31975;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=NADP-dependent alcohol dehydrogenase C;
DE EC=1.1.1.2;
GN Name=adhC; Synonyms=adh; OrderedLocusNames=MT3130;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH;
CC Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AE000516; AAK47460.1; -; Genomic_DNA.
DR PIR; H70860; H70860.
DR RefSeq; WP_003415965.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQC4; -.
DR SMR; P9WQC4; -.
DR EnsemblBacteria; AAK47460; AAK47460; MT3130.
DR GeneID; 45427038; -.
DR KEGG; mtc:MT3130; -.
DR PATRIC; fig|83331.31.peg.3373; -.
DR HOGENOM; CLU_026673_20_2_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding; NADP; Oxidoreductase; Zinc.
FT CHAIN 1..346
FT /note="NADP-dependent alcohol dehydrogenase C"
FT /id="PRO_0000426800"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 37075 MW; 969179113DBA27C1 CRC64;
MSTVAAYAAM SATEPLTKTT ITRRDPGPHD VAIDIKFAGI CHSDIHTVKA EWGQPNYPVV
PGHEIAGVVT AVGSEVTKYR QGDRVGVGCF VDSCRECNSC TRGIEQYCKP GANFTYNSIG
KDGQPTQGGY SEAIVVDENY VLRIPDVLPL DVAAPLLCAG ITLYSPLRHW NAGANTRVAI
IGLGGLGHMG VKLGAAMGAD VTVLSQSLKK MEDGLRLGAK SYYATADPDT FRKLRGGFDL
ILNTVSANLD LGQYLNLLDV DGTLVELGIP EHPMAVPAFA LALMRRSLAG SNIGGIAETQ
EMLNFCAEHG VTPEIELIEP DYINDAYERV LASDVRYRFV IDISAL