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Database: UniProt
Entry: F4WDJ9_ACREC
LinkDB: F4WDJ9_ACREC
Original site: F4WDJ9_ACREC 
ID   F4WDJ9_ACREC            Unreviewed;       691 AA.
AC   F4WDJ9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0000313|EMBL:EGI67779.1};
DE   Flags: Fragment;
GN   ORFNames=G5I_03652 {ECO:0000313|EMBL:EGI67779.1};
OS   Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS   echinatior).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN   [1] {ECO:0000313|EMBL:EGI67779.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nygaard S., Zhang G.;
RT   "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT   adaptations to social evolution and fungus farming.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; GL888087; EGI67779.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4WDJ9; -.
DR   STRING; 103372.F4WDJ9; -.
DR   EnsemblMetazoa; XM_011052551.1; XP_011050853.1; LOC105143944.
DR   eggNOG; KOG0238; Eukaryota.
DR   InParanoid; F4WDJ9; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
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   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.700.40; -; 1.
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   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_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; PF00364; Biotin_lipoyl; 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   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00867; CPSASE_2; 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}; Reference proteome {ECO:0000313|Proteomes:UP000007755}.
FT   DOMAIN          18..465
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          137..335
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          614..689
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGI67779.1"
SQ   SEQUENCE   691 AA;  77222 MW;  96B65C3217B62BC1 CRC64;
     QLTSYAQNSH QSVSQINKIN KILIANRGEI ACRITKTAKK LGIKTVAVYS EADRNSMHVE
     QADEAYCIGP AQSSQSYLRK DKIISVVKQA KCQAVHPGYG FLSENTEFAQ LCQKENIIFI
     GPPATAIRDM GIKNTSKAIM TKAGVPIIEG YHGDDQTNET LLVEARKIGF PLMIKAVRGG
     GGKGMRIAQK ESDFVEALES ARTESEKAFG DSAVLLEKYV TEPRHVEVQI FADKHGNAVF
     LFERDCSVQR RHQKVIEEAP APGISQQLRQ ELGEAAVRAA KAVGYVGAGT VEFIMDRNNH
     SFHFMEMNTR LQVEHPITEA ITGLDLVEWQ LRVASGEKLP LKQEQITLNG HAFEARIYAE
     NPRNGFLPGA GHLLYLKPPE ATDNVRVETG VRQNDEVSVH YDPMIAKLVV WGKDRSEALN
     VLISKLSEYN IAGLDTNIQF IKDLCKHSKF QSGEVHTGFI EENFEQLFPK LHISNKILIQ
     GTLASILYED IESLSTSLET KDPFTPFAVE TGLRLNHVLN RTFFFYVEKE NNIVEVKYIE
     PDIYLMRVNR LGPWRKVTGT LKKTDGALEL FTEIDGIIIK ARTVKLNNKL YIFTKDREWQ
     LIIPTPKFVT AITSQAEQNP YTALSPMPGL VDKIFINKGD VVKKGDSLLV IVAMKMEHII
     KASIDGIIED VLCSVGDNIS KNKLLVKLTK C
//
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