ID A0A7L0PK40_9AVES Unreviewed; 677 AA.
AC A0A7L0PK40;
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:NXL05198.1};
GN ORFNames=MESCAY_R07925 {ECO:0000313|EMBL:NXL05198.1};
OS Mesembrinibis cayennensis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Aequornithes; Pelecaniformes;
OC Threskiornithidae; Mesembrinibis.
OX NCBI_TaxID=1118748 {ECO:0000313|EMBL:NXL05198.1, ECO:0000313|Proteomes:UP000574277};
RN [1] {ECO:0000313|EMBL:NXL05198.1, ECO:0000313|Proteomes:UP000574277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-001-44 {ECO:0000313|EMBL:NXL05198.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXL05198.1};
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:NXL05198.1}.
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DR EMBL; VXAT01009641; NXL05198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L0PK40; -.
DR Proteomes; UP000574277; 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:UP000574277};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 3..449
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 122..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 595..670
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXL05198.1"
FT NON_TER 677
FT /evidence="ECO:0000313|EMBL:NXL05198.1"
SQ SEQUENCE 677 AA; 74651 MW; 8C658D0E3E02B2EF CRC64;
GDNIGKILIA NRGEIACRVM RTAKRMGVKS VAVYSEADRN SMHVAMADEA YCIGPAPSQQ
SYLAMEKIMQ VAKVSAAQAI HPGYGFLSEN TEFAELCKQE GIIFIGPPSS AIRDMGIKST
SKAIMSAAGV PVVEGYHGED QSDECLKEHA KRIGYPVMIK AVRGGGGKGM RIAHSEKEFL
DQLESARREA KKSFNDDAML IEKFVDNPRH VEVQVFGDQH GNAVYLFERD CSVQRRHQKI
IEEAPGPGIN PEVRKRLGEA AVKAAKAVNY VGAGTVEFIM DSQHNFYFME MNTRLQVEHP
VTEMITGTDL VEWQLRVAAG EKIPLMQEEI LLRGHAFEAR IYAEDPNNNF MPGAGPLLHL
STPPPDSFTR IETGVRQGDE VSVHYDPMIA KLVVWAEDRQ AALRKLRYSL HQYNIVGLST
NIDFLLSLSG HPQFEAGNVH TNFIPQHHDE LFPTKKATPH AVVCQAALGL ILKEKMLTDA
FRDQSDDKFS PFASSTGRRI NMCYTRKVSL LDGENIVDVA VSYNQEGSYN MQIQDETFLI
SGEIFNEGDS VYLKSSVNGK VCKSKLVILD NTIYLFFPEG SAQIGLPVPK YLSAVSSVGT
QSGAVAPMTG TVEKVFVKAG DKVQIGDPLM VMIAMKMEHT IRAPKAGVIK KVNFQEGAQA
NRHAPLVEFV DEEAESK
//
