ID A1UIA9_MYCSK Unreviewed; 588 AA.
AC A1UIA9;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Short-chain dehydrogenase/reductase SDR {ECO:0000313|EMBL:ABL92567.1};
GN OrderedLocusNames=Mkms_3373 {ECO:0000313|EMBL:ABL92567.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL92567.1};
RN [1] {ECO:0000313|EMBL:ABL92567.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL92567.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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DR EMBL; CP000518; ABL92567.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UIA9; -.
DR STRING; 189918.Mkms_3373; -.
DR ESTHER; mycss-q1b6r6; Epoxide_hydrolase.
DR KEGG; mkm:Mkms_3373; -.
DR HOGENOM; CLU_511581_0_0_11; -.
DR OrthoDB; 4220752at2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd05233; SDR_c; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43391:SF12; OXIDOREDUCTASE EPHD-RELATED; 1.
DR PANTHER; PTHR43391; RETINOL DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 161..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..283
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 588 AA; 64114 MW; F910497E17B82E3C CRC64;
MSRPAPRFVD STDGVRVAVY EEGNPDGPTV ILVHGWPDSH VVWDSVAAEL ADRFHVVRYD
NRGVSPTSAP KRAAAYTTAR YADDFAAVAD AVAPGRRVHV VAHDWGSTGM WEYLSRPEAA
DRVASYTSLS GPSVDHVYRY VLDGLKRPYR IRRLARALNQ FARLSYMILL SVPLVAPVLV
RAFIAEGLRK YQRVAEGIPA DRLLHSDTYR ADAARSVKVY RANYFRSLLT KRTPRVVDVP
VQLIVNTGDA FIRPYVYDEI APWVPTLWRR ELRAGHWSPM SHPHVIARAV AELVEHVDGA
PAARELRRAR VGGPREYFSD TLVSVTGAGS GIGRETALAF AREGAELVVS DIDEASAKET
AAAIEAAGGV AHAYRLDVAD ADAVERFADE VCAGHGIPDI VVNNAGVGQA GRFLDTPRDQ
WDHVLDVNLG GVVNGCRAFA RRLVERGTGG HIVNVASMAS YAPLQSLNAY CTSKAAVYMF
SDCLRAELDE AGIGLTTICP STVDTNIVRN TRIHAPADRT GDVAGRRGQL QKMFAMRRYG
PDKAAKAIVA AVKANKAIRP VMPEAYFVYG VSRVLPQALR STARGRVL
//
