MCCA_ARATH
ID MCCA_ARATH Reviewed; 734 AA.
AC Q42523; Q9SA61;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial;
DE Short=MCCase subunit alpha;
DE EC=6.4.1.4;
DE AltName: Full=3-methylcrotonyl-CoA carboxylase 1;
DE AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha;
DE Flags: Precursor;
GN Name=MCCA; OrderedLocusNames=At1g03090; ORFNames=F10O3.9, F10O3_8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=7716229; DOI=10.1104/pp.107.3.1013;
RA Weaver L.M., Lebrun L., Franklin A., Huang L., Hoffman N., Wurtele E.S.,
RA Nikolau B.J.;
RT "Molecular cloning of the biotinylated subunit of 3-methylcrotonyl-coenzyme
RT A carboxylase of Arabidopsis thaliana.";
RL Plant Physiol. 107:1013-1014(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=10681539; DOI=10.1074/jbc.275.8.5582;
RA McKean A.L., Ke J., Song J., Che P., Achenbach S., Nikolau B.J.,
RA Wurtele E.S.;
RT "Molecular characterization of the non-biotin-containing subunit of 3-
RT methylcrotonyl-CoA carboxylase.";
RL J. Biol. Chem. 275:5582-5590(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Biotin-attachment subunit of the 3-methylcrotonyl-CoA
CC carboxylase, an enzyme that catalyzes the conversion of 3-
CC methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for
CC leucine and isovaleric acid catabolism. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-(2E)-butenoyl-CoA + ATP + hydrogencarbonate = 3-
CC methyl-(2E)-glutaconyl-CoA + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:13589, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57344,
CC ChEBI:CHEBI:57346, ChEBI:CHEBI:456216; EC=6.4.1.4;
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC 3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC -!- SUBUNIT: Probably a heterodimer composed of biotin-containing alpha
CC subunits and beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q42523-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q42523-2; Sequence=VSP_008910;
CC -!- TISSUE SPECIFICITY: In roots, cotyledons, leaves, flowers, ovaries,
CC siliques and embryos. {ECO:0000269|PubMed:10681539}.
CC -!- MISCELLANEOUS: Temporal and spatial accumulation of the alpha and beta
CC subunits during development at approximately equal molar ratios.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to exon skipping. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25800.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U12536; AAA67356.1; -; mRNA.
DR EMBL; AC006550; AAD25800.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27527.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27528.1; -; Genomic_DNA.
DR EMBL; AY070723; AAL50065.1; -; mRNA.
DR PIR; G86161; G86161.
DR RefSeq; NP_563674.1; NM_100191.4. [Q42523-2]
DR RefSeq; NP_849583.1; NM_179252.3. [Q42523-1]
DR AlphaFoldDB; Q42523; -.
DR SMR; Q42523; -.
DR BioGRID; 23601; 2.
DR STRING; 3702.AT1G03090.2; -.
DR iPTMnet; Q42523; -.
DR PaxDb; Q42523; -.
DR PRIDE; Q42523; -.
DR ProteomicsDB; 238893; -. [Q42523-1]
DR EnsemblPlants; AT1G03090.1; AT1G03090.1; AT1G03090. [Q42523-2]
DR EnsemblPlants; AT1G03090.2; AT1G03090.2; AT1G03090. [Q42523-1]
DR GeneID; 838362; -.
DR Gramene; AT1G03090.1; AT1G03090.1; AT1G03090. [Q42523-2]
DR Gramene; AT1G03090.2; AT1G03090.2; AT1G03090. [Q42523-1]
DR KEGG; ath:AT1G03090; -.
DR Araport; AT1G03090; -.
DR TAIR; locus:2007559; AT1G03090.
DR eggNOG; KOG0238; Eukaryota.
DR InParanoid; Q42523; -.
DR OMA; FRANLGQ; -.
DR OrthoDB; 254436at2759; -.
DR PhylomeDB; Q42523; -.
DR BioCyc; ARA:AT1G03090-MON; -.
DR BRENDA; 6.4.1.4; 399.
DR UniPathway; UPA00363; UER00861.
DR PRO; PR:Q42523; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42523; baseline and differential.
DR Genevisible; Q42523; AT.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IDA:TAIR.
DR GO; GO:0006552; P:leucine catabolic process; IDA:TAIR.
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 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; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Biotin; Ligase; Manganese;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..734
FT /note="Methylcrotonoyl-CoA carboxylase subunit alpha,
FT mitochondrial"
FT /id="PRO_0000002835"
FT DOMAIN 37..484
FT /note="Biotin carboxylation"
FT DOMAIN 156..354
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 657..733
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT REGION 645..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 329
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 699
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT VAR_SEQ 281..300
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7716229"
FT /id="VSP_008910"
FT CONFLICT 85
FT /note="V -> D (in Ref. 1; AAA67356)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="A -> AK (in Ref. 1; AAA67356)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="W -> L (in Ref. 1; AAA67356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 734 AA; 80451 MW; 251CACF6464B046B CRC64;
MSMMTVWALR RNVRRKNHSM LVRYISGSAS MKPKEQCIEK ILVANRGEIA CRIMRTAKRL
GIQTVAVYSD ADRDSLHVKS ADEAVRIGPP SARLSYLSGV TIMEAAARTG AQAIHPGYGF
LSESSDFAQL CEDSGLTFIG PPASAIRDMG DKSASKRIMG AAGVPLVPGY HGHEQDIDHM
KSEAEKIGYP IIIKPTHGGG GKGMRIVQSG KDFADSFLGA QREAAASFGV NTILLEKYIT
RPRHIEVQIF GDKHGNVLHL YERDCSVQRR HQKIIEEAPA PNISEKFRAN LGQAAVSAAR
AVGYYNAGTV EFIVDTESDQ FYFMEMNTRL QVEHPVTEMI VGQDLVEWQI RVANGEPLPL
SQSEVPMSGH AFEARIYAEN VPKGFLPATG VLNHYRPVAV SPSVRVETGV EQGDTVSMHY
DPMIAKLVVW GGNRGEALVK LKDCLSNFQV AGVPTNINFL QKLASHKEFA VGNVETHFIE
HHKSDLFADE SNPAATEVAY KAVKHSAALV AACISTIEHS TWNESNHGKV PSIWYSNPPF
RVHHEAKQTI ELEWNNECEG TGSNLISLGV RYQPDGSYLI EEGNDSPSLE LRVTRAGKCD
FRVEAAGLSM NVSLAAYLKD GYKHIHIWHG SEHHQFKQKV GIEFSEDEEG VQHRTSSETS
SHPPGTIVAP MAGLVVKVLV ENEAKVDQGQ PILVLEAMKM EHVVKAPSSG SIQDLKVKAG
QQVSDGSALF RIKG
