ID A0A495ACN4_9BACI Unreviewed; 327 AA.
AC A0A495ACN4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 9.
DE SubName: Full=Alpha-ketoacid dehydrogenase subunit beta {ECO:0000313|EMBL:RKQ37737.1};
GN ORFNames=D8M06_02740 {ECO:0000313|EMBL:RKQ37737.1};
OS Oceanobacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=930130 {ECO:0000313|EMBL:RKQ37737.1, ECO:0000313|Proteomes:UP000269301};
RN [1] {ECO:0000313|EMBL:RKQ37737.1, ECO:0000313|Proteomes:UP000269301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23996 {ECO:0000313|EMBL:RKQ37737.1,
RC ECO:0000313|Proteomes:UP000269301};
RX PubMed=26869142; DOI=.1099/ijsem.0.000952;
RA Amoozegar M.A., Bagheri M., Makhdoumi A., Nikou M.M., Fazeli S.A.S.,
RA Schumann P., Sproer C., Sanchez-Porro C., Ventosa A.;
RT "Oceanobacillus halophilus sp. nov., a novel moderately halophilic
RT bacterium from a hypersaline lake.";
RL Int. J. Syst. Evol. Microbiol. 66:1317-1322(2016).
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:RKQ37737.1}.
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DR EMBL; RBZP01000001; RKQ37737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495ACN4; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000269301; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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:UP000269301}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 327 AA; 36000 MW; F569CD6BA7537D0A CRC64;
MAVMSYIQAV TTALREEMLR DEKVFILGED VGKKGGVFRA TEGLFDEFGE YRVLDTPLTE
SAIAGVGIGA AMYGMRPVAE MQFADFIMPA VNQIISEAAK TRYRSNNDWN VPITIRAPYG
GGVHGALYHS QSVESVFANQ PGLKIVMPST PYDVKGLLKA AIRDNDPVLF FEHKRAYRLL
KEDVPEEDYV LPIGKADVKR EGSDITVITY GLCVHFALQA AEKLAEEGID AHILDLRTVY
PLDKAAIIEA ASKTGKVLLI TEDNKEGSII GEVAAIIAEN CLFDLDAPIM RLAGPDVPAM
PYAPTMERYF MVNPEKCEKA MRDLAEF
//