ID D5AXL8_RICPP Unreviewed; 665 AA.
AC D5AXL8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=propionyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013050};
DE EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
GN Name=accC {ECO:0000313|EMBL:ADE30157.1};
GN OrderedLocusNames=rpr22_CDS596 {ECO:0000313|EMBL:ADE30157.1};
OS Rickettsia prowazekii (strain Rp22).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=449216 {ECO:0000313|EMBL:ADE30157.1, ECO:0000313|Proteomes:UP000006931};
RN [1] {ECO:0000313|EMBL:ADE30157.1, ECO:0000313|Proteomes:UP000006931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rp22 {ECO:0000313|EMBL:ADE30157.1,
RC ECO:0000313|Proteomes:UP000006931};
RX PubMed=20368341; DOI=10.1101/gr.103564.109;
RA Bechah Y., El Karkouri K., Mediannikov O., Leroy Q., Pelletier N.,
RA Robert C., Medigue C., Mege J.L., Raoult D.;
RT "Genomic, proteomic, and transcriptomic analysis of virulent and avirulent
RT Rickettsia prowazekii reveals its adaptive mutation capabilities.";
RL Genome Res. 20:655-663(2010).
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; CP001584; ADE30157.1; -; Genomic_DNA.
DR RefSeq; WP_004599170.1; NC_017560.1.
DR AlphaFoldDB; D5AXL8; -.
DR GeneID; 57569743; -.
DR KEGG; rpq:rpr22_CDS596; -.
DR PATRIC; fig|449216.3.peg.627; -.
DR HOGENOM; CLU_000395_3_1_5; -.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000006931; Chromosome.
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, ECO:0000313|EMBL:ADE30157.1};
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 5..451
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 124..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 588..665
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 665 AA; 73307 MW; 6A796566E30CAFA7 CRC64;
MTKPLFDKIL IANRSEIAVR IIRTLKKMGI GSVAVYSEAD TNSMYVQHAD EAYYIGDSPA
TASYLSVKNL ISAIRESGAS AVHPGYGFLS ENPNFANILK REGVVLIGPS AGTIKKMGDK
IEAKKIAIEA GVSTVPGYMG TIKDVKQAID IAKEIGFPVI VKATAGGGGR GMRVVNNPAE
MANAFESAKL EAANSFSDDR LFIEKLIQTP RHIEIQLIAD QYGNSVCLGE RECSIQRHHQ
KVIEEAPSSF ITENIRHEMY RQVISLSQKV GYYSAGTVEF IVDSNKNFYF LEMNTRLQVE
HPVTELITGI DIVEEMIKIA AGKKLSFTQD DIKLKGWAFE SRICAENPSR GFLPSSGRII
AYSEPAKSPN IRIDTGIGLG GEVSMFYDSM IAKLCTYGET REQAIEVMRS ALSSYIINGI
AHNISFLEAV MLHPRFVSGD ISTAFIQEEY PDGFSGASLT SEVTTVFLAT AIFIYISEQR
RASLISGNIN NQANKIGTRW VVTIDDKLFP VLITPVENGY NIRHESDRIY IRSNWNLGNE
LFTAMINGKK TNVKIENIRT GYLLSHAGIS VKAFVRSPRI SELEALMVSK VVLEENSELQ
APLSGQIAAI KVKEGQEVTI GQEIMILTAM KMENLILAER DGKIAKIFVN EKDNVVRGKI
LLEFA
//
