ID A0A1S3FRG3_DIPOR Unreviewed; 732 AA.
AC A0A1S3FRG3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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|RefSeq:XP_012878457.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012878457.1};
RN [1] {ECO:0000313|RefSeq:XP_012878457.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012878457.1};
RG RefSeq;
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 RefSeq; XP_012878457.1; XM_013023003.1.
DR STRING; 10020.ENSDORP00000012175; -.
DR GeneID; 105990567; -.
DR KEGG; dord:105990567; -.
DR CTD; 5095; -.
DR InParanoid; A0A1S3FRG3; -.
DR OrthoDB; 1129179at2759; -.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000081671; Unplaced.
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; 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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..732
FT /note="Propionyl-CoA carboxylase alpha chain,
FT mitochondrial"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010356603"
FT DOMAIN 62..512
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 181..378
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 656..732
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 732 AA; 80563 MW; 50A6A476FC56CD29 CRC64;
MAGLWVGAVA LVAAGGRGRR PPPQWMRSAG LWTLKHVPPY SRQCLVLSRS LGSGGCDPNE
KTFDKILIAN RGEIACRVIK TCKKMGIKTV AIHSDVDASS VHVKMADEAV CVGPAPTSKS
YLNMDAIMEA IKKTRAQAVH PGYGFLSENK DFAKRLAAED VIFIGPDTHA IQAMGDKIES
KLLAKQAKVN TIPGFDGVVK DADEAVKIAK EIGYPVMIKA SAGGGGKGMR IAWNDEETRD
GFRFSSQEAA SSFGDDRLLI EKFIDNPRHI EIQVLGDKHG NALWINEREC SIQRRNQKVV
EEAPSTFLDP KTRRAMGEQA VALAKAVKYS SAGTVEFLVD SRKNFYFLEM NTRLQVEHPV
TECITGLDIV QEMIRVAKGY PLRHKQADIP INGWAIECRV YAEDPYKSFG LPSIGRLSQY
EEPIHLPGVR VDSGIQPGSE ISIYYDPMIS KLVTYGSDRT EALKRMEDAL DNYVIRGNIH
NRSLMEYLFL NXXXLRTIET QMLTLYMTDX LMNLFPLGHI LSKSEKNQLL AIASSLFVVS
QLRARNFHQH SRVPVVKSDI GTWELCIKLR DEQHAALASN SGSTFCVEVG GSKLKLTSTW
NLALPLLSVS VDGTQRTVQC LSREAGGRMS IQFLGTVYKV HVFTKLAAEL NKFMPEKVAE
DTSSTLRSPM PGVVVAVSVK PGDMVAEGQE ICVIEAMKMQ NSMTAGKTGK VKLVHCKTGD
TVGEGDLLVE LE
//
