ID A4BZ87_9FLAO Unreviewed; 817 AA.
AC A4BZ87;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Acetoin dehydrogenase (TPP-dependent) beta chain {ECO:0000313|EMBL:EAR12480.1};
GN ORFNames=PI23P_07640 {ECO:0000313|EMBL:EAR12480.1};
OS Polaribacter irgensii 23-P.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=313594 {ECO:0000313|EMBL:EAR12480.1, ECO:0000313|Proteomes:UP000003053};
RN [1] {ECO:0000313|EMBL:EAR12480.1, ECO:0000313|Proteomes:UP000003053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23-P {ECO:0000313|EMBL:EAR12480.1,
RC ECO:0000313|Proteomes:UP000003053};
RA Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR12480.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAOG01000002; EAR12480.1; -; Genomic_DNA.
DR RefSeq; WP_004570148.1; NZ_CH724148.1.
DR AlphaFoldDB; A4BZ87; -.
DR STRING; 313594.PI23P_07640; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_350462_0_0_10; -.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000003053; Unassembled WGS sequence.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
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; PF00676; E1_dh; 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); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003053}.
FT DOMAIN 483..657
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 817 AA; 91945 MW; 6B91C3011B06C4A9 CRC64;
MSQKTLTQDK KELSFNAFKT EVLEDYKIAK ISRECSLLGR REVLTGKAKF GIFGDGKEVP
QLAMAKAFKK GDFRSGYYRD QTFMMAIGEL TAQQFFAGLY AHTNIEIEPM SAGRQMGGHF
ATHSLHEDGS WKNLTEQYNS SADISPTAGQ MPRLLGLAQA SKVYRNEKSV QHKTNFSNKG
NEVAWGTIGN ASTSEGLFFE TINAAGVLQV PMVMSVWDDE YGISVHAKHQ TTKESISEIL
KGFQRDKDSN GYEIFVVNGW DYVQLVDVYN KAGQIAREEH VPILIHVNEL TQPQGHSTSG
SHERYKGKER LQWEKEHDCL EKMRKWILDF ELATDSGEIL RFVDSEEEII LLEKEAKKIV
ITAKRNAWNA YNNEFTAEVQ VASKLLSRIA NKSKNGVFIT KYKTDLEKTA DPITKDILIA
VRKTLRYLKE EEFPEKKELQ EYIKAILKDA AHKYSSYLLS ESDYSAVKIV EKKPIYAQNK
NVVDARVVMR DNFDALLKKH PEVIIFGEDA GFIGDVNQGL EGLQEKYGDI RVSDTGIREA
TIIGQGIGLA MRGLRPIAEI QYLDYLLYAL QIMSDDLATL HYRSFGKQKA PLIIRTRGHR
LEGIWHAGSP MGGIINNIRG MHVLVPRNMN KAAGFYNTLL EGDEPALVIE CLNGYRLKEE
LPTNLGEFKT PIGLVETVRE GTDITIVSYG STLRIVEETA AELQQIGINI EIIDAQSLLP
FDLNSDCVKS LQKTNKLLVI DEDVPGGASA YILQEILEKQ NGYQYLDSKP ATLTAKAHRP
AYGTDGDYFS KPSAEDIFEK IYEIMHESNP ALFKSLY
//
