ID G9E6N4_9HYME Unreviewed; 186 AA.
AC G9E6N4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Acetyl-coenzyme A carboxylase {ECO:0000313|EMBL:AEV43003.1};
DE Flags: Fragment;
GN Name=ACC {ECO:0000313|EMBL:AEV43003.1};
OS Macrocentrus sp. BJS-2011.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Ichneumonoidea; Braconidae;
OC Macrocentrinae; Macrocentrus.
OX NCBI_TaxID=1097062 {ECO:0000313|EMBL:AEV43003.1};
RN [1] {ECO:0000313|EMBL:AEV43003.1}
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; JF980021; AEV43003.1; -; Genomic_DNA.
DR AlphaFoldDB; G9E6N4; -.
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:AEV43003.1"
FT NON_TER 186
FT /evidence="ECO:0000313|EMBL:AEV43003.1"
SQ SEQUENCE 186 AA; 20199 MW; F8AEAFD3ECABD204 CRC64;
MTLWAGWGHG SENPKLPELL HKHEIAFIGP SERAMWALGD KIASSIVAQT ADVPTLPWSG
SELKAHYSGK KIKISSELFK KGCVSTVEES LAAAKKIGFP VMVKASEGGG GKGIRKVENA
EELPALFRQV QAEVPGSPIF IMKLAKCARH LEVQLLADNY GNAISLFGRD CSIQRRHQKI
IEEALA
//