ID A0A1J5L6T0_9PROT Unreviewed; 694 AA.
AC A0A1J5L6T0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=propionyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013050};
DE EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
GN ORFNames=BM562_16175 {ECO:0000313|EMBL:OIQ26851.1};
OS Alphaproteobacteria bacterium MedPE-SWcel.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1860092 {ECO:0000313|EMBL:OIQ26851.1, ECO:0000313|Proteomes:UP000183546};
RN [1] {ECO:0000313|EMBL:OIQ26851.1, ECO:0000313|Proteomes:UP000183546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MedPE-SWcel {ECO:0000313|EMBL:OIQ26851.1};
RX PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT Associated Bacteria from the Mediterranean Sea.";
RL Front. Microbiol. 7:996-996(2016).
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}.
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:OIQ26851.1}.
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DR EMBL; MPDC01000031; OIQ26851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5L6T0; -.
DR STRING; 1860092.BM562_16175; -.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000183546; Unassembled WGS sequence.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..478
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 615..694
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 694 AA; 75122 MW; 813125B742A22D2C CRC64;
MFDKILIANR GEIACRVIKT ARKMGIKTVA IYSDADRQAL HVQMADEAVH VGPPPANQSY
IVIDKVMAAI RESGAQAVHP GYGFLSENSK FAAALAAEGV AFVGPPVGAI EKMGDKITSK
KIAQEAGVST VPGYMGLIAD ADEAVKISGE VGYPVMIKAS AGGGGKGMRI AWNDEEAREG
FQSSKNEAAS SFGDDRIFIE KFVTQPRHIE IQVLCDAHGN GIYLGERECS IQRRNQKVVE
EAPSPFLDEA TRKAMGEQAV ALAKAVGYAS AGTVEFIVDG DKNFYFLEMN TRLQVEHPVT
ELITGVDLVE QMIRVAAGQP LSIAQDDVKL TGWAIENRLY AEDPYRGFLP SIGRLTRYRP
PAEVAAGPML DAGTWNFAED ARTDGWELRG PSAETAAVRN DTGVFEGGEI SMYYDPMIAK
LCTWAPTRAA AIEAMRVALD SFEVEGIGHN LPFLSAVMDH PKFISGDITT AFIAEEYPEG
FDGATLPVAE LRRIAAACAA MHRIAEIRRT QVSGRMDNHE RRVGNHWVVD LGGQSFKTVI
AADPAGATVT FQEDDSVIRV TSDWTPGDMI AHIETEGAPL VLKVDKITQG FRIRNRGADL
KVHVRRPRQA ELAALMPEKL PPDTSKMLLC PMPGLVVKVD VAVGDEVHEG QALCTIEAMK
MENILRAEKK AVVTKVNAGA GDSLAVDDVI MEFE
//
