ID A0A0E3XPR5_MYCCH Unreviewed; 670 AA.
AC A0A0E3XPR5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:AKC40088.1};
GN ORFNames=GR01_18055 {ECO:0000313|EMBL:AKC40088.1};
OS Mycobacteroides chelonae (Mycobacterium chelonae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacteroides.
OX NCBI_TaxID=1774 {ECO:0000313|EMBL:AKC40088.1, ECO:0000313|Proteomes:UP000033056};
RN [1] {ECO:0000313|EMBL:AKC40088.1, ECO:0000313|Proteomes:UP000033056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35752 {ECO:0000313|EMBL:AKC40088.1,
RC ECO:0000313|Proteomes:UP000033056};
RX PubMed=26021923;
RA Hasan N.A., Davidson R.M., de Moura V.C., Garcia B.J., Reynolds P.R.,
RA Epperson L.E., Farias-Hesson E., DeGroote M.A., Jackson M., Strong M.;
RT "Draft Genome Sequence of Mycobacterium chelonae Type Strain ATCC 35752.";
RL Genome Announc. 3:e00536-15(2015).
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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DR EMBL; CP010946; AKC40088.1; -; Genomic_DNA.
DR RefSeq; WP_046254588.1; NZ_MLCH01000004.1.
DR AlphaFoldDB; A0A0E3XPR5; -.
DR GeneID; 31681253; -.
DR PATRIC; fig|1774.35.peg.3666; -.
DR HOGENOM; CLU_026975_0_0_11; -.
DR OrthoDB; 9810734at2; -.
DR Proteomes; UP000033056; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd05263; MupV_like_SDR_e; 1.
DR CDD; cd05233; SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR44196; DEHYDROGENASE/REDUCTASE SDR FAMILY MEMBER 7B; 1.
DR PANTHER; PTHR44196:SF5; POSSIBLE MULTI-FUNCTIONAL ENZYME WITH ACYL-COA-REDUCTASE ACTIVITY ACRA1; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 5..227
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
SQ SEQUENCE 670 AA; 74155 MW; 774BED7927AE160A CRC64;
MKYIVTGGTG FIGRRIVTRI LETQRNAEVA VLVRRESLSR FEKLAEQWDD RVQPLVGDLT
QPDLGLPTEG DPVTADHIVH CAAIYDITVD DKAQRAANVE GTRSVIGLAK RTGATLHHIS
SIAVAGSYQG EFTEEDFDVN QDLPTPYHQT KFEAELLVRS EPGLRYRIYR PAVVVGDSKT
GEMDKIDGPY YFFGILAKLA RLPRFTPMML PKAGRSNIVP VDYVVDATVE LMHQEGRDGQ
AFHLTNPEVT YLRDIYSGIA PAAGLPPVRG SLPHAIATPF LNARGTLKVW RNMVVTQLGI
PPEVIDITEI MPTFVSESTQ EALRPSGITV PSFGSYAGKL YQYWRKNLDP ERYRRDDPAG
PLVGRHVIIT GASSGIGRAA AIAVAQRGGT VFAVARDAEA LDSLVAEIRE DGGQAYSFRC
DLTDYSAVDD TVKSILGQFG HVDYLVNNAG RSIRRSAINT VDRFHDYERV MAINYFGAVR
LVLALLPHWR ERKFGHVVNV STAGVQTRNP KYASYIPTKA ALDAFSDVVA TETVSDHITF
TNIHMPLVKT PMIQPSHKLN VVPGLTPEHA AAMVIRGLVE KPTRIDHPMG TYADIGRYMT
PKLTRRIMHQ MYLAYPDSRA ARGLEPVDER QDVSTSRRRP RAAKRVAAVS KLRIPGPVMR
AVRLIPGVHW
//
