ID G1R8H2_NOMLE Unreviewed; 662 AA.
AC G1R8H2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 67.
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};
GN Name=PCCA {ECO:0000313|Ensembl:ENSNLEP00000009509.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000009509.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000009509.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000009509.2}
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; ADFV01053755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01053756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01053757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01053758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01053759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01053760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01053761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01053762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01053763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01053764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1R8H2; -.
DR Ensembl; ENSNLET00000009964.3; ENSNLEP00000009509.2; ENSNLEG00000007811.3.
DR eggNOG; KOG0238; Eukaryota.
DR GeneTree; ENSGT00940000156083; -.
DR HOGENOM; CLU_000395_3_2_1; -.
DR TreeFam; TF354220; -.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000001073; Chromosome 5.
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:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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; 2.
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; 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:UP000001073};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 62..490
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 181..359
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 585..662
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 662 AA; 72671 MW; AC96FBA5A304FAE7 CRC64;
MAGLWVGTAS LVAVGRRGRW PPQQLMLSAA LRTLKHVPYY SRQCLMVSRN LGSVGYDPNE
KTFDKILIAN RGEIACRVIR TCKKMGIKTV AIHSDVDASS VHVKMADEAV CVGPAPTSKS
YLNMDAIMEA IKKTRAQAVH PGYGFLSENK EFARCLAAED VIFIGPDTHA IQAMGDKIES
KLLAKKAEVN TIPGFDGVVK SELLSNSSLL LGYPVMIKAS AGGGGKEILH GENINHHLLC
GCGYMVFQMV LLFQVLGDKH GNALWLNERE CSIQRRNQKV VEEAPSIFLD AETRRAMGEQ
AVALARAVKY SSAGTVEFLV DSKKNFYFLE MNTRLQVEHP VTECITGLDL VQEMIRVAKG
YPLRHKQADI RVNGWAVECR VYAEDPYKSF GLPSIGRLSQ YQEPLHLPGV RVDSGIQPGS
DISIYYDPMI SKLITYGSDR TEALKRMADA LDNYVIRGVT HNIALLREVI VNSRFVKGDI
STKFLSDVYP DGFKGHMLTK SEKNQLLAIA SSLFVAFQLR AQHFQENSRM PVIKPDIANW
ELSIKLHDEV HSVVASNNGS TFSVEVDGSK LNVTSTWNLA SPLLSVSVDG TQRTVQCLSR
EAGGNMSIQF LGTVVAEGQE ICVIEAMKMQ NSMTAGKTGT VKSVHCQAGD TVGEGDLLVE
LE
//
