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Database: UniProt
Entry: A0A1M3LMF6_9PROT
LinkDB: A0A1M3LMF6_9PROT
Original site: A0A1M3LMF6_9PROT 
ID   A0A1M3LMF6_9PROT        Unreviewed;       247 AA.
AC   A0A1M3LMF6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:OJX71884.1};
GN   ORFNames=BGO92_04375 {ECO:0000313|EMBL:OJX71884.1};
OS   Magnetospirillum sp. 64-120.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=1895778 {ECO:0000313|EMBL:OJX71884.1, ECO:0000313|Proteomes:UP000184435};
RN   [1] {ECO:0000313|EMBL:OJX71884.1, ECO:0000313|Proteomes:UP000184435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=64-120 {ECO:0000313|EMBL:OJX71884.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OJX71884.1}.
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DR   EMBL; MKVK01000035; OJX71884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3LMF6; -.
DR   STRING; 1895778.BGO92_04375; -.
DR   Proteomes; UP000184435; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd05233; SDR_c; 1.
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; PTHR42760:SF106; PROTEIN FIXR; 1.
DR   PANTHER; PTHR42760; SHORT-CHAIN DEHYDROGENASES/REDUCTASES FAMILY MEMBER; 1.
DR   Pfam; PF13561; adh_short_C2; 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;
SQ   SEQUENCE   247 AA;  26339 MW;  A3DF86213933C7F2 CRC64;
     MSDAAPKTVV ITGASRGIGH SIARRFLAEG WRIITCARAE APPECKRDKN WVHHVPTDLA
     DPASTQAFVV EANRFLDGAP LHALVNNAGI SPKTPYKERL GVLNGPIDGW KEVFELNFFA
     PLRLARGFAS ALHKGKGAVV NITSIAGHYV HPFAGSAYST SKAALSGLTR EMAAELAQLG
     VRVNAVAPGE ISTAMISAEY EALVPRIPLD RMGSPEDVAG TVFRLCGDDF AYVTGSEIFV
     TGGQHLY
//
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