GenomeNet

Database: UniProt
Entry: Q42523
LinkDB: Q42523
Original site: Q42523 
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   13-FEB-2019, entry version 170.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Wurtele E.S., Nikolau B.J.;
RT   "Molecular cloning of the biotinylated subunit of 3-methylcrotonyl-
RT   coenzyme 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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RP   BY 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-methylbut-2-enoyl-CoA + ATP + hydrogencarbonate = ADP +
CC         H(+) + phosphate + trans-3-methylglutaconyl-CoA;
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-
CC       hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC   -!- SUBUNIT: Probably a heterodimer composed of biotin-containing
CC       alpha 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         Note=May be due to exon skipping. No experimental confirmation
CC         available.;
CC   -!- TISSUE SPECIFICITY: In roots, cotyledons, leaves, flowers,
CC       ovaries, siliques and embryos. {ECO:0000269|PubMed:10681539}.
CC   -!- MISCELLANEOUS: Temporal and spatial accumulation of the alpha and
CC       beta subunits during development at approximately equal molar
CC       ratios.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD25800.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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   UniGene; At.24059; -.
DR   ProteinModelPortal; Q42523; -.
DR   SMR; Q42523; -.
DR   BioGrid; 23601; 1.
DR   STRING; 3702.AT1G03090.2; -.
DR   iPTMnet; Q42523; -.
DR   PaxDb; Q42523; -.
DR   PRIDE; Q42523; -.
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   eggNOG; COG4770; LUCA.
DR   HOGENOM; HOG000008989; -.
DR   InParanoid; Q42523; -.
DR   KO; K01968; -.
DR   OMA; TEFRAHI; -.
DR   OrthoDB; 254436at2759; -.
DR   PhylomeDB; Q42523; -.
DR   BioCyc; ARA:AT1G03090-MONOMER; -.
DR   BRENDA; 6.4.1.4; 399.
DR   Reactome; R-ATH-196780; Biotin transport and metabolism.
DR   Reactome; R-ATH-70895; Branched-chain amino acid catabolism.
DR   UniPathway; UPA00363; UER00861.
DR   PRO; PR:Q42523; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   Genevisible; Q42523; AT.
DR   GO; GO:0022626; C:cytosolic ribosome; IDA: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; IDA: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; 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   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; Complete proteome; Ligase;
KW   Manganese; Metal-binding; Mitochondrion; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transit peptide.
FT   TRANSIT       1     25       Mitochondrion. {ECO:0000255}.
FT   CHAIN        26    734       Methylcrotonoyl-CoA carboxylase subunit
FT                                alpha, mitochondrial.
FT                                /FTId=PRO_0000002835.
FT   DOMAIN       37    484       Biotin carboxylation.
FT   DOMAIN      156    354       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      657    733       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   ACT_SITE    329    329       {ECO:0000250}.
FT   METAL       311    311       Manganese 1. {ECO:0000250}.
FT   METAL       325    325       Manganese 1. {ECO:0000250}.
FT   METAL       325    325       Manganese 2. {ECO:0000250}.
FT   METAL       327    327       Manganese 2. {ECO:0000250}.
FT   BINDING     152    152       ATP. {ECO:0000250}.
FT   BINDING     236    236       ATP. {ECO:0000250}.
FT   BINDING     271    271       ATP. {ECO:0000250}.
FT   MOD_RES     645    645       Phosphoserine.
FT                                {ECO:0000244|PubMed:19376835}.
FT   MOD_RES     699    699       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
FT   VAR_SEQ     281    300       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:7716229}.
FT                                /FTId=VSP_008910.
FT   CONFLICT     85     85       V -> D (in Ref. 1; AAA67356).
FT                                {ECO:0000305}.
FT   CONFLICT     92     92       A -> AK (in Ref. 1; AAA67356).
FT                                {ECO:0000305}.
FT   CONFLICT    430    430       W -> L (in Ref. 1; AAA67356).
FT                                {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
//
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