ID   A0A024K1G6_9MYCO        Unreviewed;       367 AA.
AC   A0A024K1G6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Oxidoreductase subunit beta {ECO:0000313|EMBL:CDO89736.1};
GN   ORFNames=BN973_04116 {ECO:0000313|EMBL:CDO89736.1};
OS   Mycobacterium triplex.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium simiae complex.
OX   NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO89736.1};
RN   [1] {ECO:0000313|EMBL:CDO89736.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO89736.1};
RX   PubMed=24874681; DOI=10.1128/genomeA.00499-14;
RA   Sassi M., Croce O., Robert C., Raoult D., Drancourt M.;
RT   "Draft Genome Sequence of Mycobacterium triplex DSM 44626.";
RL   Genome Announc. Announc.2:e00499-e00414(2014).
RN   [2] {ECO:0000313|EMBL:CDO89736.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO89736.1};
RA   Xu Y.W., Yang Q.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; HG964446; CDO89736.1; -; Genomic_DNA.
DR   RefSeq; WP_036470429.1; NZ_LQPY01000030.1.
DR   AlphaFoldDB; A0A024K1G6; -.
DR   STRING; 47839.BN973_04116; -.
DR   eggNOG; COG1013; Bacteria.
DR   HOGENOM; CLU_048564_1_0_11; -.
DR   OrthoDB; 9775140at2; -.
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}.
FT   DOMAIN          82..229
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          16..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   367 AA;  39581 MW;  F66090B0D1C50C69 CRC64;
     MTSGIAGDLA GTDLGLTPRL KKNDGVPRLS AEDQPQKGKD FTSDQEVRWC PGCGDYVILN
     TIRNFLPDLG LRRENIVFIS GIGCSSRFPY YLETYGFHSI HGRAPAIATG LALSREDLSV
     WVVTGDGDAL SIGGNHLIHA LRRNVNITIL LFNNRIYGLT KGQYSPTSEV GKITKSTPMG
     SLDHPFNPVS LALGAEATFV GRALDSDRAG LTEVLRGAAE HRGAAVVEIL QDCPIFNDGS
     FDALRKEGAE DRVINVRHGE PIVFGANGEY CVVKSGFSLE AAKTADVAVE EIVKHDAHTD
     DPAYAFALSR LSDQNLDHTV LGIFRDVSRP TYDDAARAQV AAARAATPYD AAALQSLLRG
     RDTWTVD
//