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Database: UniProt
Entry: A0A1H6X098_9ACTN
LinkDB: A0A1H6X098_9ACTN
Original site: A0A1H6X098_9ACTN 
ID   A0A1H6X098_9ACTN        Unreviewed;       331 AA.
AC   A0A1H6X098;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:SEJ18152.1};
GN   ORFNames=SAMN05443287_103244 {ECO:0000313|EMBL:SEJ18152.1};
OS   Micromonospora phaseoli.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1144548 {ECO:0000313|EMBL:SEJ18152.1, ECO:0000313|Proteomes:UP000198707};
RN   [1] {ECO:0000313|Proteomes:UP000198707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7038 {ECO:0000313|Proteomes:UP000198707};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FNYV01000003; SEJ18152.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6X098; -.
DR   STRING; 1144548.SAMN05443287_103244; -.
DR   OrthoDB; 151996at2; -.
DR   Proteomes; UP000198707; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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        305..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   331 AA;  35107 MW;  01AC328DB69A7A90 CRC64;
     MPLARRLADA TVVITGASSG IGTATAYALA RRGSTVVLAA RTEPALREVA RHCRELGGRT
     LVVPTDVTDP AAVHRLAATA AAEFGRIDAW INNAAVGTVG LFDEIPLAEL RRVLEVNLLG
     TAHGMRAALP HLGAAGGGVL VNNASVLAEV AMPYQSAYNA AKHGIRGLAD TVRQELRITG
     RSAISVCTVL PATIDTPFFR HAANHSGRQL VPPPPLYPPE VVAETIVRLL YRPRREAYAG
     GAARLIGLQW RLAPALAERI LGWYAQRTQF GPAPEWESTG NVFQPDGTAM PEGGWHGRRR
     QLVRITAFGL AAAGTAVGTV AAMTRRARSP R
//
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