ID B8KY50_9GAMM Unreviewed; 729 AA.
AC B8KY50;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Dehydrogenase/transketolase family protein {ECO:0000313|EMBL:EED34623.1};
GN ORFNames=NOR51B_561 {ECO:0000313|EMBL:EED34623.1};
OS Luminiphilus syltensis NOR5-1B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Luminiphilus.
OX NCBI_TaxID=565045 {ECO:0000313|EMBL:EED34623.1, ECO:0000313|Proteomes:UP000004699};
RN [1] {ECO:0000313|Proteomes:UP000004699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NOR51-B {ECO:0000313|Proteomes:UP000004699};
RX PubMed=23705883;
RA Spring S., Riedel T., Sproer C., Yan S., Harder J., Fuchs B.M.;
RT "Taxonomy and evolution of bacteriochlorophyll a-containing members of the
RT OM60/NOR5 clade of marine gammaproteobacteria: description of Luminiphilus
RT syltensis gen. nov., sp. nov., reclassification of Haliea rubra as
RT Pseudohaliea rubra gen. nov., comb. nov., and emendation of Chromatocurvus
RT halotolerans.";
RL BMC Microbiol. 13:118-118(2013).
CC -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC CO(2). {ECO:0000256|ARBA:ARBA00003906}.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; DS999411; EED34623.1; -; Genomic_DNA.
DR RefSeq; WP_009019371.1; NZ_DS999411.1.
DR AlphaFoldDB; B8KY50; -.
DR STRING; 565045.NOR51B_561; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_1_6; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000004699; 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 CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
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:UP000004699};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 394..575
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 729 AA; 79353 MW; C2482F883BB47366 CRC64;
MSDANQLNDK LRRRMQAGDY AVGDVGRAGL TNAAAIGIFR AQCMSRHLDR IARNLQKNGK
SFYTIGSSGH ENMAAVAESL RDDDMAFLHY RDAAFQIRRA MRVPGSTPLQ DMLLSFTCSS
EDPISGGRHK VLGSRSLAIP PQTSTIASHL PKAVGAAYSI DMPRGVNRGL HPLRRDSIVA
CTFGDASANH STAQGAINTA AWMGYRGLRL PILFVCEDNG IGISVPTPEG WIASSFQHRP
GLRYFYADGL NAYDAYAVAR EAVEHVREQR QPAFLHLSMV RLLGHAGSDP EISYRSSEDI
ASDEQQDPIL HTARLIADRG ILDGSALLAI YDQVGAQCEA IAAQAAVRPH LASATDVMRS
IVPPRRAVAP ASIVSPDERR KAFGREWNNI EQPQPMAKLL NWCLLDLLLE HQEIFLVGQD
IGKKGGVYGV TQKLQQRFRA GRVMDSLLDE QSILGLAIGA AHNGFLPIPE IQFLAYIHNA
EDQLRGEAAT LSFFSNGQFT NPMVVRVAGL AYQRGFGGHF HNDNSLGVLR DIPGLIVACP
SSGRDAVAML RESVRLAREE QRIVVFLEPI ALYNTRDLHE DGDNAWSSAY PEATYTAPFG
EVAQRGNGPL AIVSYGNGYY LANQASRTLE REYGIDTCLI DLRWLAPLPV DSLIKAIGSS
EHVLVVDECR RSGNVSEAIM AHLHEAGLQR IARLTAEDCF IPTGPAYAAT LPSCAAIVET
ALALLGKES
//
