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Database: UniProt
Entry: C7PQ03_CHIPD
LinkDB: C7PQ03_CHIPD
Original site: C7PQ03_CHIPD 
ID   C7PQ03_CHIPD            Unreviewed;       916 AA.
AC   C7PQ03;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-NOV-2018, entry version 46.
DE   SubName: Full=2-oxoglutarate dehydrogenase, E1 subunit {ECO:0000313|EMBL:ACU64241.1};
DE            EC=1.2.4.2 {ECO:0000313|EMBL:ACU64241.1};
GN   OrderedLocusNames=Cpin_6840 {ECO:0000313|EMBL:ACU64241.1};
OS   Chitinophaga pinensis (strain ATCC 43595 / DSM 2588 / NCIB 11800 / UQM
OS   2034).
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales;
OC   Chitinophagaceae; Chitinophaga.
OX   NCBI_TaxID=485918 {ECO:0000313|EMBL:ACU64241.1, ECO:0000313|Proteomes:UP000002215};
RN   [1] {ECO:0000313|Proteomes:UP000002215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43595 / DSM 2588 / NCIB 11800 / UQM 2034
RC   {ECO:0000313|Proteomes:UP000002215};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Sims D., Meinche L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Chitinophaga pinensis DSM 2588.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACU64241.1, ECO:0000313|Proteomes:UP000002215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43595 / DSM 2588 / NCIB 11800 / UQM 2034
RC   {ECO:0000313|Proteomes:UP000002215};
RX   PubMed=21304681; DOI=10.4056/sigs.661199;
RA   Glavina Del Rio T., Abt B., Spring S., Lapidus A., Nolan M., Tice H.,
RA   Copeland A., Cheng J.F., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Chain P., Saunders E., Detter J.C., Brettin T., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Lucas S.;
RT   "Complete genome sequence of Chitinophaga pinensis type strain (UQM
RT   2034).";
RL   Stand. Genomic Sci. 2:87-95(2010).
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DR   EMBL; CP001699; ACU64241.1; -; Genomic_DNA.
DR   RefSeq; WP_012794404.1; NC_013132.1.
DR   ProteinModelPortal; C7PQ03; -.
DR   STRING; 485918.Cpin_6840; -.
DR   EnsemblBacteria; ACU64241; ACU64241; Cpin_6840.
DR   KEGG; cpi:Cpin_6840; -.
DR   eggNOG; ENOG4105C7P; Bacteria.
DR   eggNOG; COG0567; LUCA.
DR   HOGENOM; HOG000259588; -.
DR   KO; K00164; -.
DR   OMA; IDMVCYR; -.
DR   OrthoDB; POG091H03SK; -.
DR   BioCyc; CPIN485918:G1GFO-6904-MONOMER; -.
DR   Proteomes; UP000002215; 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   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; PTHR23152; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 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; SSF52518; 2.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002215};
KW   Oxidoreductase {ECO:0000313|EMBL:ACU64241.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002215}.
FT   DOMAIN      581    774       Transket_pyr. {ECO:0000259|SMART:
FT                                SM00861}.
SQ   SEQUENCE   916 AA;  103299 MW;  8D49B789D03111EA CRC64;
     MKDFSFVTNS HPAYIESLYQ DYRKDPGAVD PEWSKFFEGF DFAVNNVNGK AGAPGAAGAG
     LPVSSDQLTK ELNVYRLIQA YRKKGHLISK TNPIRERKDR QANLDISFYG LGEADLKTEF
     YAGQVLGLGK TSLETIVNRL KQVYAASVGL EFTYINDAKK VEWLQKEMET TFQQPTTLES
     KKRILLKLNQ GVMFERFLHT KYIGQKRFGL EGGENTIPAL DAIINTAADA GVQEAVIGMA
     HRGRLNVLAN ILGKTYEQIF NEFEGHAVPD LTMGSGDVKY HLGFRSIVTT PSGKKVNLQL
     LPNPSHLEVV DPLVTGFARS KADVIYGSDY DKILPILIHG DAAVAGQGVI YELLQMSNLK
     GYYTGGTMHL VINNQIGFTT DFDDARSSDY CTSIASTVQA PVFHVNGDDA EAVVKVAEIS
     ARYRQEFNSD IFIDLLCYRK HGHNEGDEPK FTQPSLYALI DKHPNPREVY TQKLLQAGEV
     EVQELAKQME KSFWADLQER LDEVRQNPLP YNYQKPEEWW AALRKSQPED FEQSPVTAIN
     EEEVKRLFGK LMEWPKEFVP LRKVEKLLQD KIKLFETEGK LDWATGELLA YASLLAEGKD
     VRMSGEDVKR GTFSHRHAIL FDENTNATYS RLGSLQDKQG QFRIYNSLLS EFAVLGFEYG
     YAMANPNTLV LWEAQYGDFA NGAQTVIDQY VSSAEQKWTT QNGLVMLLPH GYEGGGPDHS
     NARPERFLQA CAEYNMIVTN ITTSANFFHA LRRQLTWQFR KPLVNFAPKA NLRHIGSYSP
     ISAFTEGGFK EVLDDEFVDD PSKVKKVLLC TGKMYFDLSE KQQKENRKDV AIVRLEQLYP
     LPVTQLEALN QKYKAATWFW VQEEPLNMGA ASYLQMNLKQ INYGVISRNP SAATATGFAK
     VHAREQLEII ETAFNI
//
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