ADHC1_MYCS2
ID ADHC1_MYCS2 Reviewed; 349 AA.
AC P0CH36; A0QR97; I7FIW6; Q9AE96;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=NADP-dependent alcohol dehydrogenase C 1;
DE Short=Ms-ADHC 1;
DE EC=1.1.1.2;
GN Name=adhc1; Synonyms=adh; OrderedLocusNames=MSMEG_1037, MSMEI_1007;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=11257547; DOI=10.1111/j.1574-6968.2001.tb10539.x;
RA Galamba A., Soetaert K., Buyssens P., Monnaie D., Jacobs P., Content J.;
RT "Molecular and biochemical characterisation of Mycobacterium smegmatis
RT alcohol dehydrogenase C.";
RL FEMS Microbiol. Lett. 196:51-56(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [5]
RP GENE DUPLICATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11739760; DOI=10.1099/00221287-147-12-3281;
RA Galamba A., Soetaert K., Wang X.M., De Bruyn J., Jacobs P., Content J.;
RT "Disruption of adhC reveals a large duplication in the Mycobacterium
RT smegmatis mc(2)155 genome.";
RL Microbiology 147:3281-3294(2001).
RN [6]
RP PUPYLATION AT LYS-210, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20094657; DOI=10.1039/b916104j;
RA Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA Barry C.E. III, Bark S., Dorrestein P.C.;
RT "Expansion of the mycobacterial 'PUPylome'.";
RL Mol. Biosyst. 6:376-385(2010).
CC -!- FUNCTION: Prefers aldehydes over alcohols.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for octanal {ECO:0000269|PubMed:11257547};
CC KM=40 uM for cinnamaldehyde {ECO:0000269|PubMed:11257547};
CC KM=53 uM for benzaldehyde {ECO:0000269|PubMed:11257547};
CC -!- INDUCTION: Has a higher specific activity when grown as a surface
CC pellicle rather than in agitated cultures (at protein level).
CC {ECO:0000269|PubMed:11257547}.
CC -!- DISRUPTION PHENOTYPE: Not essential for growth, strains missing one
CC copy or both grow slower and have a different morphology than wild-
CC type. {ECO:0000269|PubMed:11739760}.
CC -!- MISCELLANEOUS: Pupylation of this protein has been demonstrated,
CC however it is unknown if the protein concerned is the product of this
CC gene, of the identical gene adhC2 (AC P0CH37), or of both genes.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AJ291708; CAC35017.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK70232.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37487.1; -; Genomic_DNA.
DR RefSeq; WP_011727367.1; NZ_SIJM01000053.1.
DR RefSeq; YP_885435.1; NC_008596.1.
DR RefSeq; YP_886664.1; NC_008596.1.
DR AlphaFoldDB; P0CH36; -.
DR SMR; P0CH36; -.
DR STRING; 246196.MSMEI_1007; -.
DR EnsemblBacteria; ABK70232; ABK70232; MSMEG_1037.
DR EnsemblBacteria; AFP37487; AFP37487; MSMEI_1007.
DR GeneID; 66733732; -.
DR KEGG; msg:MSMEI_1007; -.
DR KEGG; msm:MSMEG_1037; -.
DR PATRIC; fig|246196.56.peg.1035; -.
DR eggNOG; COG1064; Bacteria.
DR OMA; YRFSIDM; -.
DR OrthoDB; 969875at2; -.
DR SABIO-RK; P0CH36; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 1: Evidence at protein level;
KW Direct protein sequencing; Isopeptide bond; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome; Ubl conjugation; Zinc.
FT CHAIN 1..349
FT /note="NADP-dependent alcohol dehydrogenase C 1"
FT /id="PRO_0000396948"
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 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CROSSLNK 210
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20094657"
FT CONFLICT 143
FT /note="Missing (in Ref. 1; CAC35017)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="P -> S (in Ref. 1; CAC35017)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="A -> R (in Ref. 1; CAC35017)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 37200 MW; D07530800034A715 CRC64;
MSTVSAYAAT SATEPLTKTT ITRRAVGPHD VAFDIHFAGI CHSDIHTVKA EWGVPNYPVV
PGHEIAGVVT EVGSEVTKYK VGDRVGVGCF VDSCRECDNC KAGLEQYCTG TGMVGTYNAI
DRDGTPTHGG YSGAIVVDEN YVLRIPDSLP LDAAAPLLCA GITTYSPLRH WNAGPGKKVA
VIGLGGLGHV AVKLAKAMGA DVTVLSQSLK KMEDGLRLGA SAYYATSDPE TFDKLAGSFD
LILNTVSANL DLGAYLGLLK LDGALVELGL PEHPMEVPAF PLLAQRRNLT GSMIGGIPET
QEMLDFCAEH DVRPEIEIIT PDYINEAYER VLASDVRYRF VIDTASLRS
