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
//