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Database: UniProt
Entry: A0A2K8PEC3_STRLA
LinkDB: A0A2K8PEC3_STRLA
Original site: A0A2K8PEC3_STRLA 
ID   A0A2K8PEC3_STRLA        Unreviewed;       356 AA.
AC   A0A2K8PEC3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=2-oxoglutarate oxidoreductase subunit KorB {ECO:0000313|EMBL:ATZ25097.1};
DE            EC=1.2.-.- {ECO:0000313|EMBL:ATZ25097.1};
DE            EC=1.2.7.3 {ECO:0000313|EMBL:QUQ54927.1};
GN   Name=korB1 {ECO:0000313|EMBL:ATZ25097.1};
GN   Synonyms=korB {ECO:0000313|EMBL:QUQ54927.1};
GN   ORFNames=SLAV_16235 {ECO:0000313|EMBL:ATZ25097.1}, SLLC_14300
GN   {ECO:0000313|EMBL:QUQ54927.1};
OS   Streptomyces lavendulae subsp. lavendulae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=58340 {ECO:0000313|EMBL:ATZ25097.1, ECO:0000313|Proteomes:UP000231791};
RN   [1] {ECO:0000313|EMBL:ATZ25097.1, ECO:0000313|Proteomes:UP000231791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 3239 {ECO:0000313|EMBL:ATZ25097.1,
RC   ECO:0000313|Proteomes:UP000231791};
RA   Busche T., Novakova R., Al'Dilaimi A., Homerova D., Feckova L.,
RA   Rezuchova B., Mingyar E., Csolleiova D., Bekeova C., Winkler A.,
RA   Sevcikova B., Kalinowski J., Kormanec J., Ruckert C.;
RT   "Complete genome sequence of Streptomyces lavendulae subsp. lavendulae CCM
RT   3239 (formerly 'Streptomyces aureofaciens CCM 3239'), the producer of the
RT   angucycline-type antibiotic auricin.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QUQ54927.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Del-LP {ECO:0000313|EMBL:QUQ54927.1};
RA   Novakova R., Ruckert C., Knirschova R., Feckova L., Busche T.,
RA   Csolleiova D., Homerova D., Rezuchova B., Javorova R., Sevcikova B.,
RA   Kalinowski J., Kormanec J.;
RT   "The linear plasmid pSA3239 is essential for the replication of the
RT   Streptomyces lavendulae subsp. lavendulae CCM 3239 chromosome.";
RL   Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP024985; ATZ25097.1; -; Genomic_DNA.
DR   EMBL; CP073778; QUQ54927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8PEC3; -.
DR   KEGG; slx:SLAV_16235; -.
DR   Proteomes; UP000231791; Chromosome.
DR   Proteomes; UP000676025; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03375; TPP_OGFOR; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR   PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ATZ25097.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231791}.
FT   DOMAIN          68..215
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   356 AA;  38770 MW;  F98906BF3EC3C627 CRC64;
     MTEVTDAPHH LLSLVPKAEA KQSMKDFKSD QEVRWCPGCG DYAVLAAVQG FMPELGLARE
     NIVFVSGIGC SSRFPYYMNT YGMHSIHGRA PAIATGLASS RRDLSVWVVT GDGDALSIGG
     NHLIHALRRN VNLKILLFNN RIYGLTKGQY SPTSEVGKIT KSTPMGSLDA PFNPVSLALG
     AEATFVARTI DSDRKHLTEV LRQAADHPGT ALVEIYQNCN IFNDGAFDAL KDQEQAREAV
     IRLEHGRPIR FGTDDTKGVT RNPDTGDLEV ITVTPDNEHR VLTHDAHATS PTTAFALSRL
     ADPDTLHHTP IGVFRDTTRP VYDTLMADQL DRAIDQKGKG DLATLLAGND TWTVVG
//
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