ID W5M5E6_LEPOC Unreviewed; 723 AA.
AC W5M5E6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Propionyl-CoA carboxylase alpha chain, mitochondrial {ECO:0000256|ARBA:ARBA00018058};
DE EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
DE AltName: Full=Propanoyl-CoA:carbon dioxide ligase subunit alpha {ECO:0000256|ARBA:ARBA00031557};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000003604.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000003604.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + butanoyl-CoA + hydrogencarbonate = (2S)-ethylmalonyl-CoA
CC + ADP + H(+) + phosphate; Xref=Rhea:RHEA:59520, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:60909, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001715};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59521;
CC Evidence={ECO:0000256|ARBA:ARBA00001715};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-
CC CoA + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23720,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57327, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:456216; EC=6.4.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000634};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23721;
CC Evidence={ECO:0000256|ARBA:ARBA00000634};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC succinyl-CoA from propanoyl-CoA: step 1/3.
CC {ECO:0000256|ARBA:ARBA00005060}.
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DR EMBL; AHAT01025041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M5E6; -.
DR STRING; 7918.ENSLOCP00000003604; -.
DR Ensembl; ENSLOCT00000003611.1; ENSLOCP00000003604.1; ENSLOCG00000003005.1.
DR eggNOG; KOG0238; Eukaryota.
DR GeneTree; ENSGT00940000156083; -.
DR HOGENOM; CLU_000395_3_3_1; -.
DR InParanoid; W5M5E6; -.
DR OMA; IGPKHYS; -.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000018468; Linkage group LG17.
DR Bgee; ENSLOCG00000003005; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.30; -; 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; 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; IPR041265; PCC_BT.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
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 Pfam; PF18140; PCC_BT; 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; PS00866; CPSASE_1; 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 Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 57..504
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 176..373
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 644..723
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 723 AA; 79481 MW; 119DE5B2AFB08F52 CRC64;
GYLATAQDSQ AAMAAYRVTP ALQRVLLALK QVSFQSRCCI IASRTHYSAV YDPNEKTFDK
ILIANRGEIA CRVIKTCKKM GIKTVAVHSD VDSGAVHVKM ADEAVCVGPA PTSKSYLNMD
AIMEAIRKTG AQAVHPGYGF LSENKEFARR LAAEGVTFIG PDTHAIQAMG DKIESKLIAK
NAKVNTIPGF DGVVKDADQA VRIAREIGYP VMIKASAGGG GKGMRIAWDD EETREGFRFS
SQEAASSFGD DRLLIEKFID NPRHIEIQVL ADKQGNALWL NERECSIQRR NQKVVEEAPS
TFLDPETRRA MGEQAVSLAR AVKYSSAGTV EFLVDSQRCF YFLEMNTRLQ VEHPITECIT
GLDLVQEMIR VAKGYALRHK QTDIPINGWA VESRVYAEDP YKSFGLPSIG RLSQYQEPVN
LSNVRVDSGI QEGSDISIYY DPMISKLVTY GSTRAEALQR MEEALDNYVI RGVTHNIPLL
REIIGHPRFV KGDISTKFLP EVYPEGFKGH QLTDSEQEEL VASAASLFVA TQLRSQRFLG
SLRVSTSQQE QKRWELSVEL EKGVHAVTVS RLGSTYTVEM GVKSLDVTSE WNLASALLPV
SINGTQRTMQ CLSRTAGGEI SLQYLGTVFK VRVLSKLAAE LSRHMPEKVP EDTSSILRSP
MPGTVVAVSV NPGDTVAEGQ EICVIEAMKM QNSMTAAKTA KVKSVHCKPG ETVGEGDLLV
ELE
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