ID N9UST3_9SPHN Unreviewed; 630 AA.
AC N9UST3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=propionyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013050};
DE EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
GN ORFNames=EBMC1_08431 {ECO:0000313|EMBL:ENY81535.1};
OS Sphingopyxis sp. MC1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1174684 {ECO:0000313|EMBL:ENY81535.1, ECO:0000313|Proteomes:UP000013072};
RN [1] {ECO:0000313|EMBL:ENY81535.1, ECO:0000313|Proteomes:UP000013072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC1 {ECO:0000313|EMBL:ENY81535.1,
RC ECO:0000313|Proteomes:UP000013072};
RA Lolas I.B., Kjeldal H., Almeida B., Le-Quy V., Gough H.L., Nielsen J.L.;
RT "Differential expression analysis of membrane associated proteins from
RT triclosan-degrading sphingopyxis.";
RL Submitted (FEB-2013) 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:ENY81535.1}.
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DR EMBL; AOUN01000005; ENY81535.1; -; Genomic_DNA.
DR RefSeq; WP_003043614.1; NZ_AOUN01000005.1.
DR AlphaFoldDB; N9UST3; -.
DR PATRIC; fig|1174684.3.peg.1703; -.
DR eggNOG; COG4770; Bacteria.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000013072; 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; 2.
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.
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:UP000013072}.
FT DOMAIN 1..421
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..314
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 551..630
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 630 AA; 68732 MW; 6050D30B912AE675 CRC64;
MFKKILIANR GEIACRVIKT ARRMGIATVA VYSDADARAP FVRMADEAVH IGPSPASESY
LIADKIIAAC KATGAEAVHP GYGFLSERTS FAEALAKENI AFIGPPVNAI AAMGDKIESK
KLAKEAGVNV VPGFVGEIRD TEHAVEISNE IGYPVMMKAS AGGGGKGMRL AYDEKDVREG
FESVKREGLN SFGDDRVFIE KFILNPRHIE IQILGDQHGN ILYLNERECS IQRRHQKVVE
EAPSPFVTEK MRKAMGEHPV TEAITGIDLV EQMIRVAAGE KLEMTQDDIK IDGWAIENRV
YAEDPYRGFL PSTGRLTRYK PPVAGWTDDG EENGRRGVDG VRVDDGVYDG GEVSIFYDPM
IAKLITWGQT RDEAADLQVA ALDRFELEGL GHNIDFVSAI MQHPRFRSGE LTTGFIAEEY
PEGFHGAPTD EAVTRALAAI AGFMASAEAD RARRTDGQLG DRLDPPAKWQ VTIDGTSHKV
KLGHKHIKVD GEKIDIALEY TPGDRLVVAE IDGSELAVKV AKTRTGWRMT TRGAIHNVRV
LPWHVAPLAS HMIEKIPPDL SKFLICPMPG LLVALHVGEG DKVEAGQPLA TVEAMKMENI
LRAEKSGVVK TVNAAQGDSL AVDAVILEME
//
