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Database: UniProt
Entry: H8K2P2_RICAG
LinkDB: H8K2P2_RICAG
Original site: H8K2P2_RICAG 
ID   H8K2P2_RICAG            Unreviewed;       665 AA.
AC   H8K2P2;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=propionyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013050};
DE            EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
GN   OrderedLocusNames=MCE_06300 {ECO:0000313|EMBL:AFC70084.1};
OS   Rickettsia amblyommatis (strain GAT-30V) (Rickettsia amblyommii).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=1105111 {ECO:0000313|EMBL:AFC70084.1, ECO:0000313|Proteomes:UP000008005};
RN   [1] {ECO:0000313|Proteomes:UP000008005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAT-30V {ECO:0000313|Proteomes:UP000008005};
RA   Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.;
RT   "Complete genome sequence of Candidatus Rickettsia amblyommii strain GAT-
RT   30V.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFC70084.1, ECO:0000313|Proteomes:UP000008005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAT-30V {ECO:0000313|EMBL:AFC70084.1,
RC   ECO:0000313|Proteomes:UP000008005};
RX   PubMed=27638476; DOI=10.1099/ijsem.0.001502;
RA   Karpathy S.E., Slater K.S., Goldsmith C.S., Nicholson W.L., Paddock C.D.;
RT   "Rickettsia amblyommatis sp. nov., a spotted fever group Rickettsia
RT   associated with multiple species of Amblyomma ticks in North, Central and
RT   South America.";
RL   Int. J. Syst. Evol. Microbiol. 66:5236-5243(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}.
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DR   EMBL; CP003334; AFC70084.1; -; Genomic_DNA.
DR   RefSeq; WP_014392597.1; NC_017028.1.
DR   AlphaFoldDB; H8K2P2; -.
DR   STRING; 1105111.MCE_06300; -.
DR   KEGG; ram:MCE_06300; -.
DR   HOGENOM; CLU_000395_3_3_5; -.
DR   OMA; FVEICSH; -.
DR   UniPathway; UPA00945; UER00908.
DR   Proteomes; UP000008005; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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          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          590..665
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   665 AA;  73301 MW;  414670A5A946F19D CRC64;
     MNKPLFDKIL IANRSEIAVR IIRTLKKMGI KSVAVYSEAD TNSMYVQHAD EAYYIGDSPA
     TESYLSIKNI ISAIRESGAS AVHPGYGFLS ENPNFANILK REGVVLIGPS AGTIKKMGDK
     IEAKKIAIEA GVSTVPGYMG TINDVKQAID IAKEIGFPVI VKAAAGGGGR GMRVVNNSAE
     MANAFESAKL EAANSFSDDR LFIEKLIQTP RHIEIQLIAD QYGNSVCLGE RECSIQRHHQ
     KVIEEAPSSF ITEDIRQEMY RQVISLSQKV GYYSAGTVEF IVDSNKNFYF LEMNTRLQVE
     HPVTELITGI DIVEEMIQIA AGEKLSFTQD DIKLKGWAFE SRICAENPSR GFLPSSGRII
     AYSEPAKSPN IRIDTGIGLG GEVSMFYDSM IAKLCTYGET REQAIELMRS ALSSYIINGI
     AHNISFLEAV MLHPRFVSGD ISTAFIQEEY PDGFSGASLT SEVTTVFLAT AIFIYISEQR
     RASLISGNIN NQANKIGTRW VVTIDDKLFP VLITPVENGY NIRHESDRIY IRSNWNLGNE
     LFTAIINGKK TNVKIENIRT GYLLSHAGIS VKAFVRSPRI SELEALMVSK VVVEESSELQ
     APLSGQIAAI KVKEGQEVTA GQEIMILTAM KMENLILAER DGKIAKIFVN EKDNVVRGQV
     LLEFA
//
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