ID A0A1C5A8X8_MICEC Unreviewed; 333 AA.
AC A0A1C5A8X8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:SCF41667.1};
GN ORFNames=GA0070618_6544 {ECO:0000313|EMBL:SCF41667.1};
OS Micromonospora echinospora (Micromonospora purpurea).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1877 {ECO:0000313|EMBL:SCF41667.1, ECO:0000313|Proteomes:UP000198253};
RN [1] {ECO:0000313|EMBL:SCF41667.1, ECO:0000313|Proteomes:UP000198253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43816 {ECO:0000313|EMBL:SCF41667.1,
RC ECO:0000313|Proteomes:UP000198253};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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DR EMBL; LT607413; SCF41667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5A8X8; -.
DR InParanoid; A0A1C5A8X8; -.
DR OrthoDB; 151996at2; -.
DR Proteomes; UP000198253; Chromosome i.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
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 PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT REGION 257..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 333 AA; 35759 MW; F94D389A867E78DA CRC64;
MTQTVVITGA SAGVGRAVAQ RYAARGARLA LIARGAAGLA AAAEDCRDRG AAEVVTHQLD
VADAGAVQRA ADEVAHRWGA LDVWINNAMV SVFAPAWEIP ADEYRRVTEV NYLGTVHGTL
AALRHMRAYR RGAVVQVGSA LAYRGIPLQS AYCASKHAVQ GFNDSLRAEL LHDCPGVKLS
MVQLPAVNTP QFSWVRTRLP RHPQPVPPIF TPEVAARAVV WAADRGPREL NVGGPTWRAR
LGNTLFPGLL DRKLARDGYD SQQTDTPVDP ATWRDNLDRP GDADRDRGAE GVFTDRARDR
SAALWVGTHK PAVTAAVLGA VALTLGGLAR RPR
//