ADHD_MYCTU
ID ADHD_MYCTU Reviewed; 368 AA.
AC P9WQB9; F2GNY2; L0TD46; O53303; Q7D655;
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=Putative alcohol dehydrogenase D;
DE EC=1.1.1.1;
GN Name=adhD; OrderedLocusNames=Rv3086;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION, AND GENE NAME.
RX PubMed=14568148; DOI=10.1016/s0378-1097(03)00648-7;
RA Singh A., Jain S., Gupta S., Das T., Tyagi A.K.;
RT "mymA operon of Mycobacterium tuberculosis: its regulation and importance
RT in the cell envelope.";
RL FEMS Microbiol. Lett. 227:53-63(2003).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Erdman;
RX PubMed=15937179; DOI=10.1128/jb.187.12.4173-4186.2005;
RA Singh A., Gupta R., Vishwakarma R.A., Narayanan P.R., Paramasivan C.N.,
RA Ramanathan V.D., Tyagi A.K.;
RT "Requirement of the mymA operon for appropriate cell wall ultrastructure
RT and persistence of Mycobacterium tuberculosis in the spleens of guinea
RT pigs.";
RL J. Bacteriol. 187:4173-4186(2005).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16893682; DOI=10.1016/j.tube.2006.01.021;
RA Cheruvu M., Plikaytis B.B., Shinnick T.M.;
RT "The acid-induced operon Rv3083-Rv3089 is required for growth of
RT Mycobacterium tuberculosis in macrophages.";
RL Tuberculosis 87:12-20(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Required for maintaining the appropriate mycolic acid
CC composition and permeability of the envelope on its exposure to acidic
CC pH. {ECO:0000269|PubMed:15937179}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
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 -!- INDUCTION: Expression is controlled by VirS. Induced at acidic pH and
CC in macrophages. {ECO:0000269|PubMed:14568148}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the mymA operon causes altered
CC cell wall structure, reduced contents and altered composition of
CC mycolic acids along with the accumulation of saturated C24 and C26
CC fatty acids, and enhanced susceptibility to antibiotics, detergents and
CC acidic pH. Also impairs ability to survive in macrophages.
CC {ECO:0000269|PubMed:15937179, ECO:0000269|PubMed:16893682}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45895.1; -; Genomic_DNA.
DR PIR; B70853; B70853.
DR RefSeq; NP_217602.1; NC_000962.3.
DR RefSeq; WP_003416075.1; NZ_NVQJ01000011.1.
DR AlphaFoldDB; P9WQB9; -.
DR SMR; P9WQB9; -.
DR STRING; 83332.Rv3086; -.
DR PaxDb; P9WQB9; -.
DR GeneID; 888654; -.
DR KEGG; mtu:Rv3086; -.
DR TubercuList; Rv3086; -.
DR eggNOG; COG1062; Bacteria.
DR OMA; VCEMSGH; -.
DR PhylomeDB; P9WQB9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central.
DR GO; GO:0010447; P:response to acidic pH; IEP:MTBBASE.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR023921; ADH_Zn_actinomycetes.
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; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03989; Rxyl_3153; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..368
FT /note="Putative alcohol dehydrogenase D"
FT /id="PRO_0000420879"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 368 AA; 38342 MW; A03FCB6F3C8003AF CRC64;
MKTTAAVLFE AGKPFELMEL DLDGPGPGEV LVKYTAAGLC HSDLHLTDGD LPPRFPIVGG
HEGSGVIEEV GAGVTRVKPG DHVVCSFIPN CGTCRYCCTG RQNLCDMGAT ILEGCMPDGS
FRFHSQGTDF GAMCMLGTFA ERATVSQHSV VKVDDWLPLE TAVLVGCGVP SGWGTAVNAG
NLRAGDTAVI YGVGGLGINA VQGATAAGCK YVVVVDPVAF KRETALKFGA THAFADAASA
AAKVDELTWG QGADAALILV GTVDDEVVSA ATAVIGKGGT VVITGLADPA KLTVHVSGTD
LTLHEKTIKG SLFGSCNPQY DIVRLLRLYD AGQLMLDELV TTTYNLEQVN QGYQDLRDGK
NIRGVIVH
