MCCB_ARATH
ID MCCB_ARATH Reviewed; 587 AA.
AC Q9LDD8; O49501; Q94F35;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial;
DE Short=MCCase subunit beta;
DE EC=6.4.1.4;
DE AltName: Full=3-methylcrotonyl-CoA carboxylase 2;
DE AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta;
DE Flags: Precursor;
GN Name=MCCB; OrderedLocusNames=At4g34030; ORFNames=F17I5.220, F28A23.210;
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 [GENOMIC DNA / MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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).
CC -!- FUNCTION: Carboxyltransferase 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 -!- 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 -!- TISSUE SPECIFICITY: In roots, cotyledons, leaves, flowers, ovaries,
CC siliques and embryos.
CC -!- MISCELLANEOUS: Temporal and spatial accumulation of the alpha and beta
CC subunits during development at approximately equal molar ratios.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA17569.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA19885.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80120.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF059511; AAF35259.1; -; Genomic_DNA.
DR EMBL; AF059510; AAF35258.1; -; mRNA.
DR EMBL; AL021961; CAA17569.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL031032; CAA19885.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161584; CAB80120.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86312.1; -; Genomic_DNA.
DR EMBL; AF386926; AAK62371.1; -; mRNA.
DR EMBL; BT000384; AAN15703.1; -; mRNA.
DR RefSeq; NP_567950.1; NM_119564.5.
DR AlphaFoldDB; Q9LDD8; -.
DR SMR; Q9LDD8; -.
DR BioGRID; 14831; 3.
DR IntAct; Q9LDD8; 1.
DR STRING; 3702.AT4G34030.1; -.
DR PaxDb; Q9LDD8; -.
DR PRIDE; Q9LDD8; -.
DR ProteomicsDB; 238373; -.
DR EnsemblPlants; AT4G34030.1; AT4G34030.1; AT4G34030.
DR GeneID; 829549; -.
DR Gramene; AT4G34030.1; AT4G34030.1; AT4G34030.
DR KEGG; ath:AT4G34030; -.
DR Araport; AT4G34030; -.
DR TAIR; locus:2124256; AT4G34030.
DR eggNOG; KOG0540; Eukaryota.
DR HOGENOM; CLU_018822_0_1_1; -.
DR InParanoid; Q9LDD8; -.
DR OMA; AYLPIMS; -.
DR OrthoDB; 632665at2759; -.
DR PhylomeDB; Q9LDD8; -.
DR BioCyc; ARA:AT4G34030-MON; -.
DR BRENDA; 6.4.1.4; 399.
DR UniPathway; UPA00363; UER00861.
DR PRO; PR:Q9LDD8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9LDD8; baseline and differential.
DR Genevisible; Q9LDD8; AT.
DR GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA: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; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0006552; P:leucine catabolic process; IDA:TAIR.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR045190; MCCB/AccD1-like.
DR PANTHER; PTHR22855; PTHR22855; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..587
FT /note="Methylcrotonoyl-CoA carboxylase beta chain,
FT mitochondrial"
FT /id="PRO_0000000292"
FT DOMAIN 68..324
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 333..579
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 68..579
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 367..396
FT /note="Acyl-CoA binding"
FT /evidence="ECO:0000255"
FT CONFLICT 143
FT /note="P -> T (in Ref. 4; AAK62371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 64013 MW; BD6E0EEFDC762955 CRC64;
MLRILGRRVV SASKELTSIQ QWRIRPGTDS RPDPFRTFRG LQKGFCVGIL PDGVDRNSEA
FSSNSIAMEG ILSELRSHIK KVLAGGGEEA VKRNRSRNKL LPRERIDRLL DPGSSFLELS
QLAGHELYEE PLPSGGIITG IGPIHGRICM FMANDPTVKG GTYYPITIKK HLRAQEIAAR
CRLPCIYLVD SGGAYLPKQA EVFPDKENFG RVFYNESVMS SDGIPQIAIV LGSCTAGGAY
IPAMADESVM VKGNGTIFLA GPPLVKAATG EEVSAEDLGG ATVHCTVSGV SDYFAQDELH
GLAIGRNIVK NLHMAAKQGM EGTFGSKNLV YKEPLYDINE LRSIAPVDHK QQFDVRSIIA
RIVDGSEFDE FKKQYGTTLV TGFARIYGQT VGIIGNNGIL FNESALKGAH FIELCSQRKI
PLVFLQNITG FMVGSRAEAN GIAKAGAKMV MAVSCAKVPK ITIITGASFG AGNYAMCGRA
YSPDFMFIWP NARIGIMGGA QAAGVLTQIE RATKKRQGIK WTEEEEEAFK KKTVDAYERE
ANPYYSTARL WDDGVIDPCD TRKVLGLCLS AALNRPLEDT RFGVFRM
