GenomeNet

Database: UniProt
Entry: Q6MC85_PARUW
LinkDB: Q6MC85_PARUW
Original site: Q6MC85_PARUW 
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
//
DBGET integrated database retrieval system