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Database: UniProt
Entry: W0Z962_9MICO
LinkDB: W0Z962_9MICO
Original site: W0Z962_9MICO 
ID   W0Z962_9MICO            Unreviewed;       327 AA.
AC   W0Z962;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000313|EMBL:CDK00307.1};
DE            EC=1.2.4.1 {ECO:0000313|EMBL:CDK00307.1};
GN   Name=pdhB {ECO:0000313|EMBL:CDK00307.1};
GN   ORFNames=MIC448_2330001 {ECO:0000313|EMBL:CDK00307.1};
OS   Microbacterium sp. C448.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1177594 {ECO:0000313|EMBL:CDK00307.1, ECO:0000313|Proteomes:UP000028883};
RN   [1] {ECO:0000313|EMBL:CDK00307.1, ECO:0000313|Proteomes:UP000028883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C448 {ECO:0000313|EMBL:CDK00307.1,
RC   ECO:0000313|Proteomes:UP000028883};
RX   PubMed=24526651; DOI=10.1128/genomeA.01113-13;
RA   Martin-Laurent F., Marti R., Waglechner N., Wright G.D., Topp E.;
RT   "Draft Genome Sequence of the Sulfonamide Antibiotic-Degrading
RT   Microbacterium sp. Strain C448.";
RL   Genome Announc. Announc.2:e01113-e01113(2014).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:CDK00307.1}.
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DR   EMBL; CBVQ010000150; CDK00307.1; -; Genomic_DNA.
DR   RefSeq; WP_036301679.1; NZ_HG779813.1.
DR   AlphaFoldDB; W0Z962; -.
DR   STRING; 1177594.MIC448_2330001; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_0_11; -.
DR   OrthoDB; 3457658at2; -.
DR   Proteomes; UP000028883; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:CDK00307.1};
KW   Pyruvate {ECO:0000313|EMBL:CDK00307.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028883}.
FT   DOMAIN          7..182
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   327 AA;  35275 MW;  0971FB35C7AF151C CRC64;
     MNAPQNMPLS KALNAGLRKA MERSDRVLMM GEDIGPLGGV FRITEGLHAE FGPNRVIDTP
     LAESGIVGTA IGLAMGGFRP VCEIQFDGFV YPAFDQITSQ LAKITNRMQG ALSMPVVIRI
     PYGGHIGAIE HHQESPEAYF THTAGLRVVS PSTPNDAYWM IQDAIFSDDP VIFLEPKSKY
     WQKGEVDLTS PPVGLHESRL VRRGTDVTLV GHGAMVTTLL QAAALAEAEG ISCEVIDLRS
     LSPVDYGPIL DSVRSTGRMV YAQEAPGFTS LGSEIAATVT ERAFYSLEAP VLRVSGFDAP
     FPPAKLEGTY LPDADRVLEA VDRALAY
//
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