ID A0A0P7HV29_9MICC Unreviewed; 350 AA.
AC A0A0P7HV29;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=2-oxoisovalerate dehydrogenase {ECO:0000313|EMBL:KPN21806.1};
GN ORFNames=AO716_01995 {ECO:0000313|EMBL:KPN21806.1};
OS Arthrobacter sp. Edens01.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1732020 {ECO:0000313|EMBL:KPN21806.1, ECO:0000313|Proteomes:UP000054460};
RN [1] {ECO:0000313|EMBL:KPN21806.1, ECO:0000313|Proteomes:UP000054460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Edens01 {ECO:0000313|EMBL:KPN21806.1,
RC ECO:0000313|Proteomes:UP000054460};
RA Couger M.B.;
RT "Draft Genome of Arthrobacter sp. strain Edens01.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPN21806.1}.
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DR EMBL; LKIU01000002; KPN21806.1; -; Genomic_DNA.
DR RefSeq; WP_055239213.1; NZ_LKIU01000002.1.
DR AlphaFoldDB; A0A0P7HV29; -.
DR STRING; 1732020.AO716_01995; -.
DR OrthoDB; 3457658at2; -.
DR Proteomes; UP000054460; 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 Reference proteome {ECO:0000313|Proteomes:UP000054460}.
FT DOMAIN 17..192
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 350 AA; 37392 MW; 7C0FDF3052AA2AEB CRC64;
MTVTAQAPAP EDTRVSLTFA KALNTALADE MAADSAVVMF GEDVGPLGGV FRITDGLTAR
FGEERCFDTP LAESGIMGMA VGMAMNGIRP VVEMQFDAFA YPAFEQVVSH VAKMSNRTRG
KVKLPLVIRI PYAGGIGGVE HHCDSSESYY AHTPGLTVLA PATVADAYTM LREAIRFPDP
VVFLEPKKLY WTKEDVDLAA LRAPFEDSTP AADPAIGKAA VAREGTDATL IAYGPSVSTA
LSAAEAAAAE GRSLEVIDIR SIVPFDDETV CASVRKTGRA VVISEAPGFA SVASEIVARI
QERCFHSLAA PVLRVTGFDI PYPAPKLEHF FLPGVDRILD AVDELQWEDK
//
