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Database: UniProt
Entry: A0A0N4VJL4_ENTVE
LinkDB: A0A0N4VJL4_ENTVE
Original site: A0A0N4VJL4_ENTVE 
ID   A0A0N4VJL4_ENTVE        Unreviewed;       596 AA.
AC   A0A0N4VJL4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0000313|WBParaSite:EVEC_0001103501-mRNA-1};
GN   ORFNames=EVEC_LOCUS10360 {ECO:0000313|EMBL:VDD95609.1};
OS   Enterobius vermicularis (Human pinworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX   NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0001103501-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EVEC_0001103501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDD95609.1, ECO:0000313|Proteomes:UP000274131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (OCT-2018) 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; UXUI01010768; VDD95609.1; -; Genomic_DNA.
DR   STRING; 51028.A0A0N4VJL4; -.
DR   WBParaSite; EVEC_0001103501-mRNA-1; EVEC_0001103501-mRNA-1; EVEC_0001103501.
DR   Proteomes; UP000038041; Unplaced.
DR   Proteomes; UP000274131; 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; 3.30.470.20; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000274131}.
FT   DOMAIN          15..458
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          134..331
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          521..594
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   596 AA;  66313 MW;  F9B3A0EBEE896F2F CRC64;
     MIGVFNVRRF STAKKISRLL IANRGEIAIR VIKTARRMGI ETVAVYSDAD RNSLHVAKAD
     FAYHIGPSSS VQSYLNIDRI IEVANKAKVQ AIHPGYGFLS ENATFAECCA KAGLIFVGPP
     PRAIRDMGAK DVSKRLMAES GVPVIRGYHG TDQSDQKLRE EATLIGYPVM LKAVYGGGGK
     GMRVVLEESE FAEKLSSARS EAHKAFGDSS MIVEKFIERP RHIEVQVFGD THDNYVYIWE
     RDCSVQRRHQ KIIEEAPAFG INAETRRKLG ETAVQASKAI GYVGAGTVEF IMDKNGQFYF
     MEMNTRLQVE HPVTEAISGL DLVEWQLRVA EGEELPLKQD QVQLGGHAIE ARIYAEDTRS
     GFLPTAGKLI HVAIPNSVRV DTGVRQGDEV TIHYDPMIAK VIAWGSNREK AIVKLQKALN
     DTHIVGVPTN IEFMIKTLGN PDFQKGDLYT DFIKDHEKEL FEEERLSEND LCDAITAYYL
     LTKPLHSRQH YKKTGILLLQ LFGEKQLQFA LPKESEVFKN EEDEKLEAHS PIPGVIERVL
     VSQGEQVKQG QALIVMIAMK MEYIIRAPSH ATVTALHCSA GDNVSKGSTL VSFASE
//
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