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
//