ID A0A087HKL8_ARAAL Unreviewed; 733 AA.
AC A0A087HKL8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=AALP_Aa1g024600 {ECO:0000313|EMBL:KFK42670.1};
OS Arabis alpina (Alpine rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK42670.1, ECO:0000313|Proteomes:UP000029120};
RN [1] {ECO:0000313|Proteomes:UP000029120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT "Genome expansion of Arabis alpina linked with retrotransposition and
RT reduced symmetric DNA methylation.";
RL Nat. Plants 1:14023-14023(2015).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CM002869; KFK42670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087HKL8; -.
DR EnsemblPlants; KFK42670; KFK42670; AALP_AA1G024600.
DR Gramene; KFK42670; KFK42670; AALP_AA1G024600.
DR eggNOG; KOG0238; Eukaryota.
DR OMA; APMHGIV; -.
DR OrthoDB; 1129179at2759; -.
DR Proteomes; UP000029120; Chromosome 1.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblPlants.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:EnsemblPlants.
DR GO; GO:0006552; P:leucine catabolic process; IEA:EnsemblPlants.
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; IPR045774; MCCA_BT_dom.
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 Pfam; PF19331; MCCA_BT; 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; PS00866; CPSASE_1; 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:UP000029120}.
FT DOMAIN 36..483
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 155..353
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 656..732
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 733 AA; 80476 MW; BEE2FA380DEE3BD6 CRC64;
MSMTVWALRR NIRRKSYSML IRYISDGVTI KPKERCIEKI LVANRGEIAC RIMRTAKRLG
IQTVAVYSDA DRDSLHVKSA DEAVRIGPPP ARLSYLSGVT IMEAAARTGA QAIHPGYGFL
SESSDFAQLC EDSGLTFIGP PASAIRDMGD KSASKRIMGA AGVPLVPGYH GHEQDIDHMK
SEAGKIGYPI IIKPTHGGGG KGMRIVESEK DFSDAFLGAQ REAAASFGVN TILLEKYITR
PRHIEVQVFG DKHGNVLHLY ERDCSVQRRH QKIIEEAPAP NISEKFRASL GQAAVSAAQA
VGYHSAGTVE FIVDTESDQF YFMEMNTRLQ VEHPVTEMIV GQDLVEWQIR VANGEPLPIS
QSEVPLSGHA FEARIYAENV PKGFLPATGV LNHYRPVGVS SSVRVETGVE QGDTVSMHYD
PMIAKLVVWG GNRGEALVKL KDCLSNFQVA GVPTNINFLQ KLASHKEFSV GNVETHFIEH
HKSDLFADES NPAAAEVAYK AVKHSAALVA ACVFSIENSD WNESNHGKLP SLWYSHPPFR
VHHEAKQTIE LEWDNEYYSN GSNLISLGLV YQPDGSYLIQ EGNDSPSLEV RVTRVGKCDF
RVEAAGLSMN VTVATYLKDG YKHIHIWQGS EHHQFKQKVG IEFSEDEEGV QHRTRSDTSA
HPPGTIVAPM AGLVVKVLVE NEAKVDQGQP ILVMEAMKME HVVKAPASGS VQDLKVKAGQ
QVSDGSALFR IQG
//
