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Database: UniProt
Entry: V9IMQ2_APICE
LinkDB: V9IMQ2_APICE
Original site: V9IMQ2_APICE 
ID   V9IMQ2_APICE            Unreviewed;       502 AA.
AC   V9IMQ2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   13-SEP-2023, entry version 34.
DE   SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:AEY61809.1};
GN   ORFNames=ACCB14117 {ECO:0000313|EMBL:AEY61809.1};
OS   Apis cerana (Indian honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Apis.
OX   NCBI_TaxID=7461 {ECO:0000313|EMBL:AEY61809.1};
RN   [1] {ECO:0000313|EMBL:AEY61809.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:AEY61809.1};
RA   Sun L., Zheng H., Wang Y., Xie X., Zhu Y., Gu W., Wang S.;
RT   "Decoding the brain transcriptome of the Eastern honeybee (Apis cerana)
RT   based on pyrosequencing.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; JR052896; AEY61809.1; -; mRNA.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   2: Evidence at transcript level;
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          31..479
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          150..348
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   502 AA;  56131 MW;  6972DB21A2CEEB70 CRC64;
     MYLMEKMSIL QCSKIISHIN NLHTSKITTG RFNKILIANR GEIACRVIKT AKRLGIQTVA
     VYSDVDKDSL HVEQADEAYY IGPAPPSQSY LRQDKIISIA KKSKCQAIHP GYGFLSENAE
     FAEFCQKENI IFIGPPANAI KNMGIKSTSK NIMTKAGIPV IAGYHGKDQS NEILLLEAKK
     IGFPLMIKAI CGGGGKGMRI ALKESEFIEA LECAKIECEN AFNDSAILLE QYINNPRHIE
     IQVFADKHGN IVHLFERDCS IQRRYQKIIE EAPAPGISAN LRSDLGTTAV QVAKTVEYIG
     AGTVEFIMDC NTNNFYFMEM NTRLQVEHPI TELITGLDLV EWQLLIAAGE ELPLKQAQIN
     FKGHAFEARI YAENPRKNFL PGAGKLSYMR IPNIRNKSIR VETGVREKDQ VSVHYDPLIA
     KLIVWGKDRE EALNILKSKL NNFNIAGIDT NIEFIKDLCS HSNFRQGKVH TGFIEEHLSK
     IXSKIQMPTH IAAQASSCLD TL
//
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