ID A6W004_MARMS Unreviewed; 701 AA.
AC A6W004;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Transketolase domain protein {ECO:0000313|EMBL:ABR72033.1};
GN OrderedLocusNames=Mmwyl1_3123 {ECO:0000313|EMBL:ABR72033.1};
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR72033.1};
RN [1] {ECO:0000313|EMBL:ABR72033.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1 {ECO:0000313|EMBL:ABR72033.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000749; ABR72033.1; -; Genomic_DNA.
DR AlphaFoldDB; A6W004; -.
DR STRING; 400668.Mmwyl1_3123; -.
DR KEGG; mmw:Mmwyl1_3123; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_1_6; -.
DR OrthoDB; 9780894at2; -.
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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 381..555
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 701 AA; 77883 MW; 85A92ACCD3DB76FB CRC64;
MNQLLEKNHR VKNVIRQKPE FDWLRVSQLM LLSRALDEIE EKELVPEKLV FNQFSARGHD
FAQILLGSLL THPHDAASGY YRSRPFVMSL GIDLDEVVAS PMAKAGGYSD GRDIGVVCNY
PNVDRKGAML FPMCGGVGAQ YTPISGWAQS ILYHKNQLND SSYAGAIAVS MGGDSSMSTN
GFWSALNIST TNNLPHLFYI EDNGYGISVP QEVQTPGGDQ VANLKAYKNL KIIDGDGTDP
ELTPVLIKEA VEYVRSGKGT CLLRLKVPRL CGHTFQDTQT YKNEDFIADE QARDPLPKLK
RYLLDNGFMT ADEWHDLEDE CYRDIRLSVD KAKERQQPDP ENLTRFVYAE KDKVQLRGGL
AASGHVFPTQ SDQAKPEGSR LNMLTAIRKT LDYELATNPK VMVFGEDVGP KGGVHGATLG
LNEKFGGDRV FDTSLSEEGI IGRSVGLALS GLMPVPEIQF RKYAEPAAEQ LSDTGIMRWR
TNNQFAAPMV VRIPGGFARR GDPWHSMSDE VEWAHKVGWQ LAMPSNAEDA VGLLRFALRD
NNPTIFFEHR SLLDNSWSRR PYPGDDYVIP FGKAKTILTG TALTVVCWGA MVERCQNAAT
NLDMSIEVID LRTIQPWDKE TVLASVEKTG RCLIVHEDNK TAGFGAEIVA TLADELFFSL
DAPIQRLTMP DIPNPHNFLL LEKAVPSEQK IADAMKKLIE V
//
