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Database: UniProt
Entry: Q5I0C3
LinkDB: Q5I0C3
Original site: Q5I0C3 
ID   MCCA_RAT                Reviewed;         715 AA.
AC   Q5I0C3;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   16-JAN-2019, entry version 106.
DE   RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0000250|UniProtKB:Q96RQ3};
DE            Short=MCCase subunit alpha {ECO:0000250|UniProtKB:Q96RQ3};
DE            EC=6.4.1.4;
DE   AltName: Full=3-methylcrotonyl-CoA carboxylase 1 {ECO:0000250|UniProtKB:Q96RQ3};
DE   AltName: Full=3-methylcrotonyl-CoA carboxylase biotin-containing subunit {ECO:0000250|UniProtKB:Q96RQ3};
DE   AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha {ECO:0000250|UniProtKB:Q96RQ3};
DE   Flags: Precursor;
GN   Name=Mccc1 {ECO:0000312|EMBL:AAH88473.1, ECO:0000312|RGD:1310615};
GN   Synonyms=Mcca {ECO:0000250|UniProtKB:Q96RQ3};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000312|EMBL:AAH88473.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Brown Norway {ECO:0000269|PubMed:15489334};
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH88473.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RA   Maurya D.K., Bhargava P.;
RL   Submitted (JAN-2009) to UniProtKB.
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         Evidence={ECO:0000250|UniProtKB:Q96RQ3};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000250|UniProtKB:Q96RQ3};
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 dodecamer composed of six biotin-containing
CC       alpha subunits (MCCC1) and six beta (MCCC2) subunits. Interacts
CC       (via the biotin carboxylation domain) with SIRT4 (By similarity).
CC       {ECO:0000250|UniProtKB:Q96RQ3, ECO:0000250|UniProtKB:Q99MR8}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q96RQ3}.
CC   -!- PTM: Acetylated. {ECO:0000250|UniProtKB:Q99MR8}.
DR   EMBL; BC088473; AAH88473.1; -; mRNA.
DR   RefSeq; NP_001009653.1; NM_001009653.1.
DR   UniGene; Rn.15587; -.
DR   ProteinModelPortal; Q5I0C3; -.
DR   SMR; Q5I0C3; -.
DR   BioGrid; 254844; 1.
DR   STRING; 10116.ENSRNOP00000018942; -.
DR   iPTMnet; Q5I0C3; -.
DR   PhosphoSitePlus; Q5I0C3; -.
DR   jPOST; Q5I0C3; -.
DR   PaxDb; Q5I0C3; -.
DR   PRIDE; Q5I0C3; -.
DR   GeneID; 294972; -.
DR   KEGG; rno:294972; -.
DR   UCSC; RGD:1310615; rat.
DR   CTD; 56922; -.
DR   RGD; 1310615; Mccc1.
DR   eggNOG; KOG0238; Eukaryota.
DR   eggNOG; COG4770; LUCA.
DR   HOGENOM; HOG000008989; -.
DR   HOVERGEN; HBG000555; -.
DR   InParanoid; Q5I0C3; -.
DR   KO; K01968; -.
DR   OrthoDB; 254436at2759; -.
DR   PhylomeDB; Q5I0C3; -.
DR   BRENDA; 6.4.1.4; 5301.
DR   UniPathway; UPA00363; UER00861.
DR   PRO; PR:Q5I0C3; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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; PS00867; CPSASE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Biotin; Complete proteome; Ligase;
KW   Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1     38       Mitochondrion. {ECO:0000250}.
FT   CHAIN        39    715       Methylcrotonoyl-CoA carboxylase subunit
FT                                alpha, mitochondrial.
FT                                /FTId=PRO_0000365095.
FT   DOMAIN       45    490       Biotin carboxylation. {ECO:0000255}.
FT   DOMAIN      163    360       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      622    711       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   ACT_SITE    335    335       {ECO:0000250|UniProtKB:P24182}.
FT   BINDING     159    159       ATP. {ECO:0000250|UniProtKB:P24182}.
FT   BINDING     243    243       ATP. {ECO:0000250|UniProtKB:P24182}.
FT   BINDING     278    278       ATP. {ECO:0000250|UniProtKB:P24182}.
FT   MOD_RES     193    193       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q99MR8}.
FT   MOD_RES     233    233       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q99MR8}.
FT   MOD_RES     490    490       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q99MR8}.
FT   MOD_RES     577    577       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q99MR8}.
FT   MOD_RES     577    577       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q99MR8}.
FT   MOD_RES     677    677       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   715 AA;  79330 MW;  20FB2EAB8664AD8F CRC64;
     MAAAALLAAV DRNQLRRVPI LLLQPREWPW KHRTVKYGTT PGGSITKVLI ANRGEIACRV
     IRTARKMGVQ SVAVYSEADR NSMHVDMADE AYSIGPAPSQ QSYLAMEKII QVAKSSAAQA
     IHPGYGFLSE NMEFAEFCKQ EGIIFIGPPS TAIRDMGIKS TSKSIMAAAG VPVVEGYHGN
     DQSDECLKEH AGKIGYPVMI KAIRGGGGKG MRIIRSEKEF QEQLESARRE AKKSFNDDAM
     LIEKFVDTPR HVEVQVFGDH HGNAVYLFER DCSVQRRHQK IIEEAPAPGI DPEVRRRLGE
     AAVRAAKAVN YVGAGTVEFI MDSKHNFYFM EMNTRLQVEH PVTEMITGTD LVEWQLRIAA
     GEKIPLSQEE IPLQGHAFEA RIYAEDPDNN FMPGAGPLVH LSTPPPDMST RIETGVRQGD
     EVSVHYDPMI AKLVVWASDR QSALSKLRYS LHQYNIVGLR TNVDFLLRLS GHSEFEAGNV
     HTDFIPQHHK DLLPTHSTIA KESVCQAALG LILKEKEMTS AFKLHTQDQF SPFSFSSGRR
     LNISYTRNMT LRSGKNDIII AVTYNRDGSY DMQIENKLFR VLGDLSNEDG YTYLKSSVNG
     VASKSKFILL DNTIYLFSME GSIEVGIPVP KYLSPVSAEG TQGGTIAPMT GTIEKVFVKA
     GDRVKAGDAL MVMIAMKMEH TIKAPKDGRI KKVFFSEGAQ ANRHAPLVEF EEEEV
//
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