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Database: UniProt
Entry: A0A384B813_BALAS
LinkDB: A0A384B813_BALAS
Original site: A0A384B813_BALAS 
ID   A0A384B813_BALAS        Unreviewed;       725 AA.
AC   A0A384B813;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial isoform X1 {ECO:0000313|RefSeq:XP_007195419.1};
GN   Name=MCCC1 {ECO:0000313|RefSeq:XP_007195419.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007195419.1};
RN   [1] {ECO:0000313|RefSeq:XP_007195419.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007195419.1};
RG   RefSeq;
RL   Submitted (JAN-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   RefSeq; XP_007195419.1; XM_007195357.1.
DR   AlphaFoldDB; A0A384B813; -.
DR   STRING; 310752.A0A384B813; -.
DR   GeneID; 103018095; -.
DR   KEGG; bacu:103018095; -.
DR   CTD; 56922; -.
DR   InParanoid; A0A384B813; -.
DR   OrthoDB; 1129179at2759; -.
DR   Proteomes; UP000261681; Unplaced.
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; 3.30.470.20; 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:UP000261681}.
FT   DOMAIN          48..494
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          167..364
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          626..715
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   725 AA;  80392 MW;  DF71E40F66996173 CRC64;
     MAAASALSVL LVAAERSRWR RVPSSLLPPR GWTWKQRAMK YATTTGRNIT KVLIANRGEI
     ACRVIRTAKK MGVQSVAVYS EADRNSMHVD MADEAHSIGP APSQQSYLSM EKIIQVAKIS
     AAQAIHPGYG FLSENMEFAE LCKQEGIIFI GPPSSAIRDM GIKSTAKSIM AAAGVPVVEG
     YHGDDQSDQC LKEHARRIGY PVMIKAVRGG GGKGMRIIRS EKEFQEQLES ARREAKKSFN
     DDAMLIEKFV DTPRHVEVQV FGDHHGNAVY LFERDCSVQR RHQKIIEEAP GPGIKPEVRK
     KLGEAAVRAA KAVNYVGAGT VEFIMDSKHN FYFMEMNTRL QVEHPVTEMI TGTDLVEWQL
     RIAAGEKIPL SQEEITLRGH AFEARIYAED PNNNFMPGAG PLVHLSTPRA DLATRIETGV
     RQGDEVSVHY DPMIAKLVVW AADRQAALTK LRYSLRQYSI VGLHTNIDFL LKLSGHPEFE
     AGNVHTDFIP QHRKELLPHR KTTAKEFLCQ AALGLILKEK AMTDVFKIQT QDQYSPFVSS
     SGRRLNICFT RNMTLRDGKN NVAIAVTYNR DGSHSMQIED KTFHVLGDLC SEGDCTYLKS
     SVNGVASKTK LIILENTIYL FSMDGSIQIG IPVPRYLSSV SSEGTQGGAV APMTGTVEKV
     FVKAGDKVKA GDSLMVMIAM KMEHTIKAPK DGTIKKVFYE EGAQANRHAP LVEFEEEESD
     KREAE
//
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