ID N1UYJ0_9MICC Unreviewed; 370 AA.
AC N1UYJ0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Pyruvate dehydrogenase E1 component, beta subunit {ECO:0000313|EMBL:EMY34130.1};
GN ORFNames=D477_011261 {ECO:0000313|EMBL:EMY34130.1};
OS Arthrobacter crystallopoietes BAB-32.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1246476 {ECO:0000313|EMBL:EMY34130.1, ECO:0000313|Proteomes:UP000010729};
RN [1] {ECO:0000313|EMBL:EMY34130.1, ECO:0000313|Proteomes:UP000010729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-32 {ECO:0000313|EMBL:EMY34130.1,
RC ECO:0000313|Proteomes:UP000010729};
RX PubMed=23833141;
RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Desai S.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Arthrobacter crystallopoietes Strain BAB-32,
RT Revealing Genes for Bioremediation.";
RL Genome Announc. 1:e00452-13(2013).
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:EMY34130.1}.
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DR EMBL; ANPE02000131; EMY34130.1; -; Genomic_DNA.
DR AlphaFoldDB; N1UYJ0; -.
DR OrthoDB; 3457658at2; -.
DR Proteomes; UP000010729; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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 Pyruvate {ECO:0000313|EMBL:EMY34130.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010729}.
FT DOMAIN 47..222
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 40012 MW; D83BD70978805785 CRC64;
MSEHATLSDL DAARDNTQSA AAQRESVEVI PAANESGQPA GPDAETLSMQ QALNRALSEI
LEADRKAVVL GEDVGQLGGV FRITDGLQRK FGEARVFDTP LAESGILGMS VGLAMAGYHP
IPEVQFDGFA YPAVNQIICQ VGRMNYRSRG KLPMPITLRV PSFGGIRAPE HHGESLEALF
AHVPGLKVVS PSTPHEAYHL LKFAASRPDP VVFMEPKSRY WQKGPVDTAA SGYSPEGARV
VREGRHLTLV AWGAMVARCL QVAELAAEDG IDIEVLDLRW LKPIDAEALA TSVGKTRRAV
VVHEAPLTSG LGAEVAALIT ERCFGTLKAP VERVTGFDVP YPSGDLEDEY IPDIDRILFG
IQRVLEYRRG
//
