GenomeNet

Database: UniProt
Entry: G9E6L2_9HYME
LinkDB: G9E6L2_9HYME
Original site: G9E6L2_9HYME 
ID   G9E6L2_9HYME            Unreviewed;       186 AA.
AC   G9E6L2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Acetyl-coenzyme A carboxylase {ECO:0000313|EMBL:AEV42981.1};
DE   Flags: Fragment;
GN   Name=ACC {ECO:0000313|EMBL:AEV42981.1};
OS   Maxfischeria sp. 1 BJS-2008.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Ichneumonoidea; Braconidae;
OC   Maxfischeriinae; Maxfischeria.
OX   NCBI_TaxID=571261 {ECO:0000313|EMBL:AEV42981.1};
RN   [1] {ECO:0000313|EMBL:AEV42981.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Sharanowski B.J., Dowling A.P.G., Sharkey M.J.;
RT   "Molecular phylogenetics of Braconidae (Hymenoptera: Ichneumonoidea) based
RT   on multiple nuclear genes and implications for classification.";
RL   Syst. Entomol. 36:549-572(2011).
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DR   EMBL; JF979999; AEV42981.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9E6L2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR   InterPro; IPR049076; ACCA.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR45728:SF3; ACETYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          1..186
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          68..159
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEV42981.1"
FT   NON_TER         186
FT                   /evidence="ECO:0000313|EMBL:AEV42981.1"
SQ   SEQUENCE   186 AA;  20302 MW;  B1BFA833C3144EDB CRC64;
     MTLWAGWGHA SENPKLPELL HKKDISFIGP SERAMWALGD KIASSIVAQT ADVPTLPWSG
     SELKAQYSGK KIKISSELFR KGCVSTIEEC LGAANKIGFP VMIKASEGGG GKGIRKVENA
     EELPTLFRQV QTEVPGSPIF IMKLAKCARH LEVQLLADNY GNAISLFGRD CSIQRRHQKI
     IEEALA
//
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