ID A0A7L0QDD1_SETKR Unreviewed; 696 AA.
AC A0A7L0QDD1;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0000256|ARBA:ARBA00070568};
DE EC=6.4.1.4 {ECO:0000256|ARBA:ARBA00026116};
DE AltName: Full=3-methylcrotonyl-CoA carboxylase 1 {ECO:0000256|ARBA:ARBA00076115};
DE AltName: Full=3-methylcrotonyl-CoA carboxylase biotin-containing subunit {ECO:0000256|ARBA:ARBA00076418};
DE AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha {ECO:0000256|ARBA:ARBA00082627};
DE Flags: Fragment;
GN Name=Mccc1 {ECO:0000313|EMBL:NXL16474.1};
GN ORFNames=SETKIR_R06340 {ECO:0000313|EMBL:NXL16474.1};
OS Setophaga kirtlandii (Kirtland's warbler) (Dendroica kirtlandii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passeroidea; Parulidae; Setophaga.
OX NCBI_TaxID=298831 {ECO:0000313|EMBL:NXL16474.1, ECO:0000313|Proteomes:UP000550059};
RN [1] {ECO:0000313|EMBL:NXL16474.1, ECO:0000313|Proteomes:UP000550059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-001-45 {ECO:0000313|EMBL:NXL16474.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXL16474.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00055202}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylbut-2-enoyl-CoA + hydrogencarbonate + ATP = 3-methyl-
CC (2E)-glutaconyl-CoA + ADP + phosphate + H(+); Xref=Rhea:RHEA:13589,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57344, ChEBI:CHEBI:57346,
CC ChEBI:CHEBI:456216; EC=6.4.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00052347};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC 3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC {ECO:0000256|ARBA:ARBA00025711}.
CC -!- SUBUNIT: Probably a dodecamer composed of six biotin-containing alpha
CC subunits (MCCC1) and six beta (MCCC2) subunits. Interacts (via the
CC biotin carboxylation domain) with SIRT4.
CC {ECO:0000256|ARBA:ARBA00065291}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXL16474.1}.
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DR EMBL; VXAS01006907; NXL16474.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L0QDD1; -.
DR Proteomes; UP000550059; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:UniProtKB-EC.
DR CDD; cd06850; biotinyl_domain; 1.
DR FunFam; 2.40.50.100:FF:000003; Acetyl-CoA carboxylase biotin carboxyl carrier protein; 1.
DR FunFam; 3.30.1490.20:FF:000003; acetyl-CoA carboxylase isoform X1; 1.
DR FunFam; 3.30.470.20:FF:000028; Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; 1.
DR FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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; IPR050856; Biotin_carboxylase_complex.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CPAse_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; NF006367; PRK08591.1; 1.
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 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; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000550059};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 22..468
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 141..338
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 600..689
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXL16474.1"
FT NON_TER 696
FT /evidence="ECO:0000313|EMBL:NXL16474.1"
SQ SEQUENCE 696 AA; 77019 MW; 4F3AEECB92023B44 CRC64;
LHRQWNQVRI FVKWASTIGG HSIGKILIAN RGEIACRVMR TAKKMGVKSV AVYSEADRNS
MHVAMADEAY CIGPPPSQQS YLAMEKILQV AKVSAAQAIH PGYGFLSENT EFAELCKQQG
IIFIGPPSSA IRDMGIKSTS KAIMSAAGVP VVEGYHGEDQ SDECLKEHAR RIGYPVMIKA
VRGGGGKGMR IAHSEKEFLD QLESARREAK KSFNDDAMLI EKFVDNPRHV EVQVFGDQHG
NAVYLFERDC SVQRRHQKII EEAPGPGISA EVRRRLGEAA VRAAKAVNYV GAGTVEFIMD
SQHNFYFMEM NTRLQVEHPV TEMITGTDLV EWQLRVAAGE KIPLMQEEIL LQGHAFEARI
YAEDPNNNFM PGAGPLLHLS TPPADRFTRI ETGVRQGDEV SVHYDPMIAK LVVWAEDRQA
ALRRLRYSLS QYNIVGLSTN IDFLLSLSGH PQFEAGNVHT NFIPQHHDEL FPAKKATPHE
VMCQAALGLI LKEKMLTDAF RDQSDDKFSP FASSTGRRLN ICYTRKLSLL DGENTVDVAV
SYNQDGSYKM QIQDKTFLIS GEILKEGDSL YLRSSVNGTV SKSKLVILDN AIYLFFPEGS
AQIGLPVPKY LSAVSSGAEQ GGAVAPMTGT VEKVFVKAGD KVQIGDPLMV MIAMKMEHTI
RAPKAAVIKK VNFQEGAQAN RHAPLVEFLD EEEESK
//
