ID A0A226ER09_FOLCA Unreviewed; 1340 AA.
AC A0A226ER09;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0000313|EMBL:OXA59587.1};
GN ORFNames=Fcan01_04334 {ECO:0000313|EMBL:OXA59587.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA59587.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA59587.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA59587.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA59587.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXA59587.1}.
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DR EMBL; LNIX01000002; OXA59587.1; -; Genomic_DNA.
DR STRING; 158441.A0A226ER09; -.
DR Proteomes; UP000198287; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000198287};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1280..1301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..453
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 588..665
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1340 AA; 150153 MW; EEF57A574926EA0C CRC64;
MAGLKQISKV LVANRGEIAC RIFRTCKKLG IRTVGVFSEP DANSQHVHMA DEAYLIGPAA
STKSYLNQDK IFEVAKRSGA HAIHPGYGFL SENSDFAKKC SDRQLIFIGP PPQAIFDMGI
KSKSKELMTA AGVPVVPGYH GQEAANDMEA LKKEALKLGF PLMIKAVKGG GGKGMRIART
AEEFLSQAQS CQSEAEKAFG DGALLIERYV EAPRHVEVQV FGDSHGNCVY LWERDCSVQR
RHQKVIEEAP ALGLTAETRK AIGTAAVNAA KAVKYTGAGT VEFIVEGQDF YFMEMNTRLQ
VEHPVTEAIT GLDLVQWQLL VAMGHELPIK NQDQIPGPFG HALEMRVYAE DTAAGFVPAP
GNVHAMRVPG GDARVESAII EGDDVSVFYD PMIAKLVIWG ENRSEAIRKA DLALSQFNVG
GVETNIDFMR RILQTNAFRN TIVTTKFIEE NHDEILVLNE LSGQQLALAT MALSAIQDYD
KSETIAGKFR MNSDYKTKFS VKDGEKKFDI GVIFNTQGSQ KVFSIGDVGE CRLIRVTKLT
EMFEMEVQIG NKRETITAAL SAENVLSVFT PDGSFKVEVP TLGPKDRVGE SGDTASGTVV
SPMPGTLEKV SVKEGEKVTK GQQLGTLVAM KMEHVIRSPY DGTVEKVHQS MGKTVAKGSN
LFTVTPFLLQ PICQSTPLPV WRNTTMARWI LIGLCIGTVI SASIPFIKAQ KMDDNDDPSN
VMISEMKDAP LRYVRGVYEV PQPPNELPVI YDTYFPVIFE FNLPKWDPAS MKIQFWKDHN
NCTESEKFSD GYPCPIMHHM NTLIANFAGN MTLWKNLFLD DPLPSDEHSS RVLLEDNPDL
DLPLVFSRNS SLILDQEYYC SKIVPHFTNF QTSRDRVDEY YKLLDKCEND LVPVVVNMSE
STVSLESMYH TTFSSFVSDY WDRLPSMISK QAVTVSVWSS LESTLLLHQY METQKWTNAI
NSCQQSQIPW TLIDHDAITS AIQSHTLFDS HQLAIPLTEM SKYFKLPLTD CVFVEKDTLV
VRVLIPVRFH AKEEEDLANK EIKSKSAYKI IKFEPIVFHE DGEFCWIDGI RNKRFVTDSA
HEGNLYVTEC NSGEGEQKLC HIPINHYSSH DAADPCAQAL YTDSEQEIVE SCVIKCLPVD
KRHFNFKYFN FAHTFDDNFI YSVADDELAV KIKCEGKKPF KIGRLNYAAW NLTLPCGCEI
TGGGPTIHFE IASPCHDNFI VEKIRPYHWR NISKKGNKTV TSSAQAASSS GGFRFNSART
EDEFVELLDQ RYGAYTLHYV TLWVIILVLS VTVGLLSYFV VQLREWRKHE LFRESRLIYS
NVDNREDFQM EGPAAQVSRY
//
