ID A0A099TDK1_9RHOB Unreviewed; 666 AA.
AC A0A099TDK1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=propionyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013050};
DE EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
GN ORFNames=PM04_06760 {ECO:0000313|EMBL:KGL02244.1};
OS Thalassobacter sp. 16PALIMAR09.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassobacter.
OX NCBI_TaxID=1225651 {ECO:0000313|EMBL:KGL02244.1, ECO:0000313|Proteomes:UP000029829};
RN [1] {ECO:0000313|EMBL:KGL02244.1, ECO:0000313|Proteomes:UP000029829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16PALIMAR09 {ECO:0000313|EMBL:KGL02244.1,
RC ECO:0000313|Proteomes:UP000029829};
RA Mas-Llado M., Nogales B., Bosch R.;
RT "Draft genome sequence of Thalassobacter sp. 16PALIMAR09.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KGL02244.1}.
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DR EMBL; JHAK01000002; KGL02244.1; -; Genomic_DNA.
DR RefSeq; WP_038004805.1; NZ_JHAK01000002.1.
DR AlphaFoldDB; A0A099TDK1; -.
DR OrthoDB; 9763189at2; -.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000029829; 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}; Reference proteome {ECO:0000313|Proteomes:UP000029829}.
FT DOMAIN 1..451
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 587..666
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 666 AA; 72823 MW; E222A1E6E0641051 CRC64;
MFEKILIANR GEIACRVIKT AKAMGIKTVA IYSDADKNAL HVKMADEAVH IGPPPANQSY
IVIDKVMEAI KQTGAQAVHP GYGFLSENSK FAEALEAAGV AFIGPPVGAI EKMGDKITSK
KIAQEANVST VPGYMGLIED AEEAVKISNQ IGYPVMIKAS AGGGGKGMRI AWNDTEAREG
FQSSKNEAAN SFGDDRIFIE KFVTQPRHIE IQVLCDSHGN GVYLHERECS IQRRNQKVVE
EAPSPFLDEA TRKAMGEQSL ALAHAVGYAS AGTVEFIVDG DRNFYFLEMN TRLQVEHPVT
ELITGVDLVE QMIRVADGEV LGIKQEDLKI KGWAIENRLY AEDPYRNFLP SIGRLTRYRP
PVEGALGDGT VRNDTGVFEG GEISMYYDPM IAKLCTWGPD RATAIETMRT ALDSFEVEGI
GHNLPFVAAV MDHDIFIKGD MTTAFIEEQY PDGFEGVTLD ETALSRVAAA CAAMHRVAEI
RRTRVSGRMD NHERKVGDDW VVTAQGARMD VTVDADKDGA TVQLKDGASL RVESDWTPGD
SLARVMIDGT PMVLKVDKMV GGFRIRFRGA DIKVHVRTPR QAELADLMPE KLPPDTSKML
LCPMPGLIVK IDVAEGEEVQ EGQALCTVEA MKMENILRAE KKGIVTKINA GPGDSLAVDE
VIMEFE
//
