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Database: UniProt/TrEMBL
Entry: W6KAX2_9PROT
LinkDB: W6KAX2_9PROT
Original site: W6KAX2_9PROT 
ID   W6KAX2_9PROT            Unreviewed;       974 AA.
AC   W6KAX2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   07-JUN-2017, entry version 14.
DE   SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:CCQ75436.1};
DE            EC=1.2.4.2 {ECO:0000313|EMBL:CCQ75436.1};
GN   Name=sucA {ECO:0000313|EMBL:CCQ75436.1};
GN   ORFNames=MGMAQ_3624 {ECO:0000313|EMBL:CCQ75436.1};
OS   Magnetospira sp. QH-2.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospira.
OX   NCBI_TaxID=1288970 {ECO:0000313|EMBL:CCQ75436.1, ECO:0000313|Proteomes:UP000032733};
RN   [1] {ECO:0000313|EMBL:CCQ75436.1, ECO:0000313|Proteomes:UP000032733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-2 {ECO:0000313|EMBL:CCQ75436.1};
RX   PubMed=23841906; DOI=10.1111/1462-2920.12180;
RA   Ji B., Zhang S.D., Arnoux P., Rouy Z., Alberto F., Philippe N.,
RA   Murat D., Zhang W.J., Rioux J.B., Ginet N., Sabaty M., Mangenot S.,
RA   Pradel N., Tian J., Yang J., Zhang L., Zhang W., Pan H., Henrissat B.,
RA   Coutinho P.M., Li Y., Xiao T., Medigue C., Barbe V., Pignol D.,
RA   Talla E., Wu L.F.;
RT   "Comparative genomic analysis provides insights into the evolution and
RT   niche adaptation of marine Magnetospira sp. QH-2 strain.";
RL   Environ. Microbiol. 16:525-544(2014).
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DR   EMBL; FO538765; CCQ75436.1; -; Genomic_DNA.
DR   RefSeq; WP_046022539.1; NZ_FO538765.1.
DR   EnsemblBacteria; CCQ75436; CCQ75436; MGMAQ_3624.
DR   KEGG; magq:MGMAQ_3624; -.
DR   KO; K00164; -.
DR   Proteomes; UP000032733; 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:UP000032733};
KW   Oxidoreductase {ECO:0000313|EMBL:CCQ75436.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032733}.
FT   DOMAIN      608    801       Transket_pyr. {ECO:0000259|SMART:
FT                                SM00861}.
SQ   SEQUENCE   974 AA;  109071 MW;  433C665B77C148F5 CRC64;
     MTPTLDTLLS GSNATYIAEL YGKYLENPGS VDATWAGFFT ELEEDGRAVL DELRGATWAP
     SGTTVIGGPG GARPTAAGPG LASGPSTSDL KRATHDSIRA LMMIRTYRVR GHLIANFDPL
     GLEGKSYHPE LDYKYYGFNE EDLDRPIFID FQLGRETATL KEILGVLKAT YCDTIGVEFM
     HMQDPEEKAW IRQRIEDLPT RHNFTHLGKR TIFQRLIEAE GFERFLDKKW KGTKRFGLDG
     GESLIAALEQ IVKRGSQLGV DDIVIGMPHR GRLNVLASVM CKPYRAIFAE FHGVASDAFS
     DVQGSGDVKY HLGVSADRVF DGTRVHLSLT ANPSHLEAVN PVVVGKVRSK QNRRGDKKRQ
     NVMGILMHGD AAFAGQGLVA ETLEMSQLEG YTTGGTIHFI VNNQIGFTTV PSKSRSSPYC
     SDVAKSIQAP IFHVNGDDPE AVVHVARLAI EFRQEFKRDV VIDMFCYRRH GHNEGDEPMF
     TQPIMYRTIA KHQRTLEVYR DRLIREGVLT QQDAETMINE FEARLEADFE TATTYRPNKA
     DWLEGVWDGL IRLNEEEELR EDDTSVPMEL LKTVGNAISR KPDNFNLHPK IARQLDAKAK
     AVDQGKGIDW ATAEALAFGT LMTEGTSVRL SGQDCGRGTF SHRHSVLIDQ VSEEKYLPLQ
     NICEGQGNYE VLDSPLSEFG VLGYEYGYSL DDPHTLVLWE AQFGDFANGA QVMIDQFISS
     GESKWMRFCG LVMLLPHGME GQGPEHSSAR LERYLQLCAE DNLQVCNITT PANYYHALRR
     QVRRNYRKPL VIMSPKSLLR HKQVISDLKD MAEGTKFRRV LPEVDKLAKN DKIRRVVLCS
     GKVYYDLLQT RRDEGLDDVA IVRVEQLYPW PRKGVMAQLA RYPKAEVVWC QEEPANMGSW
     TFVLPRLAHI LQSLGLSQTL PFYAGRCAAA SPATGFAKVH AAEQAQLVNE ALNIAPDDLP
     QPFRPPAKPS DRRC
//
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