ID L0J799_9MYCO Unreviewed; 367 AA.
AC L0J799;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Mycothiol-dependent formaldehyde dehydrogenase {ECO:0000313|EMBL:AGB26758.1};
GN ORFNames=Mycsm_06630 {ECO:0000313|EMBL:AGB26758.1};
OS Mycobacterium sp. JS623.
OG Plasmid pMYCSM01 {ECO:0000313|EMBL:AGB26758.1,
OG ECO:0000313|Proteomes:UP000010844}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB26758.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|EMBL:AGB26758.1, ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|EMBL:AGB26758.1,
RC ECO:0000313|Proteomes:UP000010844};
RC PLASMID=pMYCSM01 {ECO:0000313|EMBL:AGB26758.1,
RC ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of plasmid 1 of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; CP003079; AGB26758.1; -; Genomic_DNA.
DR AlphaFoldDB; L0J799; -.
DR KEGG; msa:Mycsm_06630; -.
DR PATRIC; fig|710686.3.peg.6679; -.
DR HOGENOM; CLU_026673_14_1_11; -.
DR Proteomes; UP000010844; Plasmid pMYCSM01.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08279; Zn_ADH_class_III; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR017816; MycoS_dep_FDH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR NCBIfam; TIGR03451; mycoS_dep_FDH; 1.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF19; RIBULOSE-5-PHOSPHATE REDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Plasmid {ECO:0000313|EMBL:AGB26758.1};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 13..367
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 367 AA; 38690 MW; 4D4430684763DFC3 CRC64;
MKEEELMSQT VRGVISRSKK QPVELVDIVI PDPGPGEVVV DIIACGVCHT DLTYREGGIN
DEYPFLLGHE AAGTVESVGE GVTHVAPGDF VILNWRAVCG ECRACKRGRP HLCFDTFNAT
QKMTLTDGTE LTPALGIGAF ADKTLVHQGQ CTKVDPEADP AVAGLLGCGV MAGLGAAINT
GAVGRDDTVA VIGCGGVGDA AIAGAALAGA RTIIAVDLDD RKLALAREFG ATHVVNAAHA
DVVKSIQDLT DGFGADVVID AVGRPATYEQ AFYARDLAGT VVLVGVPTPD MQLQLPLVDF
FSRGGALKSS WYGDCLPERD FPTLISLYRQ GRLPLQKFVS ERIGLDAIED AFHKMHVGEV
LRSVVVL
//
