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Database: UniProt
Entry: K1Q095_CRAGI
LinkDB: K1Q095_CRAGI
Original site: K1Q095_CRAGI 
ID   K1Q095_CRAGI            Unreviewed;       630 AA.
AC   K1Q095;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000313|EMBL:EKC27353.1};
GN   ORFNames=CGI_10001206 {ECO:0000313|EMBL:EKC27353.1};
OS   Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC27353.1};
RN   [1] {ECO:0000313|EMBL:EKC27353.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC27353.1};
RX   PubMed=22992520; DOI=10.1038/nature11413;
RA   Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA   Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA   Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA   Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA   Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA   Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA   Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA   Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA   Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA   Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA   Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT   "The oyster genome reveals stress adaptation and complexity of shell
RT   formation.";
RL   Nature 490:49-54(2012).
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC       carboxyl carrier protein, biotin carboxylase and 2 subunits each of
CC       ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
CC       {ECO:0000256|ARBA:ARBA00011842}.
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DR   EMBL; JH817215; EKC27353.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1Q095; -.
DR   HOGENOM; CLU_434306_0_0_1; -.
DR   InParanoid; K1Q095; -.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR030664; SdhA/FrdA/AprA.
DR   InterPro; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   NCBIfam; TIGR01811; sdhA_Bsu; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF53; SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   ACT_SITE        330
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   630 AA;  69075 MW;  EEC08602F0D89C93 CRC64;
     MRLDSKVPKG PLAEKWSNHK FSMKLVNPAN RRKHKVIVVG TGLAGSSAAA SLSEMGYNVH
     VFCIHDTPRR AHSIAAQGGI NAAKNYQNDG DSVYRLFYDT IKGGDYRSRE ANVYRLAEVS
     VNIIDQCVAQ GVPFAREYGG LLDNRSFGGA QVSRTFYARG QTGQQLLLGA YAAMSKEIGK
     GGVTLYPRSE MLDLVVVDGV ARGVIIRDLL SGEIKCHSAD VVLLCTGGYG NVYYLSTNAK
     ACNVSATFRA YKRGAGFANP CYVQIHPTCI PVAGEFQSKL TLMSESLRND GRVWVPKKDG
     ETRSATQIPE DERDYFLERK YPSFGNLVPR DVASRNAKVM CDEGRGVGLS KQAVYLDFSD
     AINRLGYDAI SAKYGNLFEM YEKITGENPY QTPMRIFPAV HYTMGVDAVT RIDITCDEGS
     FVQTGKKIVS KDPLSFSDKQ GDYKTKIKQT REKLGIDDAI IYGTGKIEQL PIVIAAMDFR
     FIGGSMGCVV GENLYRAMSL AIKKKYPLLV FSCSGGARMQ EGLLSLMQMA KTCAGAENMN
     NAKVPFLSIF THPTMGGVTA SFASVADVMI GEPGAHIGFA GPRVIEQTVK QKLPPDFQTS
     EFLLENGFLD MVVHRTELRK TITQLIRFLS
//
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