ID Q6MC85_PARUW Unreviewed; 890 AA.
AC Q6MC85;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN ORFNames=PC_RS05260 {ECO:0000313|EMBL:CAF23814.1};
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Protochlamydia.
OX NCBI_TaxID=264201 {ECO:0000313|EMBL:CAF23814.1, ECO:0000313|Proteomes:UP000000529};
RN [1] {ECO:0000313|EMBL:CAF23814.1, ECO:0000313|Proteomes:UP000000529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25 {ECO:0000313|EMBL:CAF23814.1,
RC ECO:0000313|Proteomes:UP000000529};
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(2004).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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; BX908798; CAF23814.1; -; Genomic_DNA.
DR RefSeq; WP_011175640.1; NC_005861.2.
DR AlphaFoldDB; Q6MC85; -.
DR STRING; 264201.pc1090; -.
DR KEGG; pcu:PC_RS05260; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_0; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000000529; Chromosome.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000529};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 550..743
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 890 AA; 101662 MW; B58344FF2AAC0E7B CRC64;
MDGHPIVEGE LANIELLENL YQDYQKKYDS LDPSWHRYFQ ELETASSFTT TNKQSSSSNH
VDHVIDVLRR DGHLISSVNP ISLNPSSFTF SLTEYLKPCV DTQAIIQTSK FEYLRKIYCD
RIGFEYKHLN DKKMEVWIQD FIEQQFFKQT LTKEQKQHVL ACLSRSELFE TFLHTKYIGQ
KRFSLEGAET LIPMLDLLIE AGAEQGVQEF LVGMAHRGRL NVLANILNKS LDTIFSEFGE
EYIPTSLEGM GDVKYHKGYT GEKIKTRLGK SIKISLSPNP SHLESVNAVV EGKTRAKQFL
AGGEKARKKI IPILIHGDAA VSGQGVVYET LQLSQLKGYE TGGTIHFVIN NQIGFTTIPR
DLRSTRYCTD IARAFGLPIF HVNAEDPDSC VQVTLLALEI RQRFHCDVFI DLNGYRKYGH
NEGDEPAYTQ PLECRLIKGK QSIRKMYYDQ LLVQGILDPQ MMDQLEAAYK AGLREVHEKI
NQPQAISSVV KQPFSIPQSF FQSVETGVNL EKLISLAERF SQIPQGFTLH PKVDYLVKER
LRQVKENKLI DWGLAEHLAY ASLLEEGVSI RISGQDCCRG TFSHRHAIWV DQHTEKDYYP
LAHLKQGQGK FEIVNSPLSE MAVLGFEYGY SVVCVKGLNV WEAQFGDFNN GAQIIIDQFI
ASAEQKWGQK SGLILFLPHG LEGQGPEHSS GRLERFLTLA GHDNLQIVNT TTPAQFFHLL
RRQVKHQFEK PLIVFTPKGL LRYPKCVSAL HEFTQGTFRE IIDDVFANPS EIKRLVLCSG
RIYYDLLAER EKLNQKEIGF IRIEQLYPLH MEELKKLIFQ YPHIQEVVWA QEEPQNMGAW
SFMFPYLNEL ISSSIQLSYV GRERSATPAT GSYCLHNQEH ANILKQVFKT
//