ID C6XTT7_PEDHD Unreviewed; 807 AA.
AC C6XTT7;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Transketolase domain protein {ECO:0000313|EMBL:ACU03723.1};
GN OrderedLocusNames=Phep_1509 {ECO:0000313|EMBL:ACU03723.1};
OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457
OS / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU03723.1, ECO:0000313|Proteomes:UP000000852};
RN [1] {ECO:0000313|EMBL:ACU03723.1, ECO:0000313|Proteomes:UP000000852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 /
RC NCIMB 9290 / NRRL B-14731 / HIM 762-3
RC {ECO:0000313|Proteomes:UP000000852};
RX PubMed=21304637; DOI=10.4056/sigs.22138;
RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.C., Saunders E., Chertkov O.,
RA Brettin T., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Pedobacter heparinus type strain (HIM 762-
RT 3).";
RL Stand. Genomic Sci. 1:54-62(2009).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP001681; ACU03723.1; -; Genomic_DNA.
DR AlphaFoldDB; C6XTT7; -.
DR STRING; 485917.Phep_1509; -.
DR KEGG; phe:Phep_1509; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_350462_0_0_10; -.
DR Proteomes; UP000000852; Chromosome.
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:UP000000852}.
FT DOMAIN 473..647
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 807 AA; 89545 MW; 2C07FC86D0F14493 CRC64;
MMPNSKLTTN PIDASELSFD DFKTIVINDY KIAVESRQAS LLGRKEVLTG KAKFGIFGDG
KELPQIAMAK AFKNGDWRSG YYRDQTFAFA AGICTIKEFF AQLYANPSVE ADPASAGRQM
NCHFATRSLN EDGSWKDLTD IKNSSSDIAP TGGQMARLVG LAYASKLYRQ NPELEYLKNF
SVNGNEVAFG TIGNASTSEG VFFEAINAAG VLQIPMAMSV WDDAYGISVP AKYQTTKEDI
SEILKGFQRD EKVEGYEIYK VRGWDYPALC ETYQRAIDVC RSEHVPVLIH VTEVTQPQGH
STSGSHERYK DKDRLEWEKE YDCILQMRKW MLESAIISEE EILELENTAK KFVRETQKEA
WNEFLASIKA EKDLVVTAIN NVANGDPALI KIASVLVSTP DAQRREVISS ARKALRLSIS
QPSAARNELL DWYNDQAGLN EDRYHSKLFT DGAESPMLVN ELKPAYNELS KMVDGRELLN
ACFDANFARD QRLVAFGEDL GAIGDVNQGF AGLQAKYGEL RITDTGIREM TIIGQGIGLA
LRGLRPIAEI QYLDYLLYAL NILSDDLASL SYRTKAGQKA PVIIRTRGHR LEGVWHSGSP
IGMILGSLRG LHICVPRNMT QAAGMYNTLF RSDEPALLIE CLNGYRLKEK LPENVGEYTV
PLGKAEVIRE GSDLTVVSYG STLRIVEEAA EELAQLGISI EIVDPQTLLP FDTDQLCAQS
LARTNKLLVV DEDVPGGGTA FLLQQILEVQ NGYYHLDGQP RTLSAKAHRP PYGSDGDYFS
KPSVDDVIEV VYAMMNESNP GKYPAIY
//
