ID I7JA77_9RICK Unreviewed; 760 AA.
AC I7JA77;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 03-MAY-2023, entry version 46.
DE RecName: Full=propionyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013050};
DE EC=6.4.1.3 {ECO:0000256|ARBA:ARBA00013050};
GN ORFNames=wOo_00540 {ECO:0000313|EMBL:CCF77923.1};
OS Wolbachia endosymbiont of Onchocerca ochengi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=100901 {ECO:0000313|EMBL:CCF77923.1, ECO:0000313|Proteomes:UP000007516};
RN [1] {ECO:0000313|EMBL:CCF77923.1, ECO:0000313|Proteomes:UP000007516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Adamawa_Cameroon {ECO:0000313|Proteomes:UP000007516};
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
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; HE660029; CCF77923.1; -; Genomic_DNA.
DR AlphaFoldDB; I7JA77; -.
DR STRING; 100901.wOo_00540; -.
DR KEGG; woo:wOo_00540; -.
DR PATRIC; fig|100901.6.peg.45; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_3_5; -.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000007516; 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; 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.
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:UP000007516}.
FT DOMAIN 4..498
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 684..760
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 760 AA; 84823 MW; 83CA63F7D244CCB8 CRC64;
MERKYCKILI ANRGEIACRI IRTAHRVGIS CVCVYSDADV NSVHVRQADE SRYIGPSPSY
LSYLNIEKIC EAAVETGVQA VHPGYGFLAE NPDFPRALQR YSIDFIGPSA ETIEVIANKI
TAKEAAKRAG VNAVPGYIGK INDAAHAASV AEEIGFPVIL KAALGGGGKG MRVVSSKKEI
ELAFISATNE AEKSFKDRSI FIEKYIELSR HIEIQIIADK YGNVVCLGER ECSVQRNNQK
IIEETPSPFI SERVRQGMYI QCVSLAKEVG YFSAGTVEFV VDKNQNFYFL EVNTRLQVEH
PVTEFVTGID IVEEMIRTSC GEKLRFSQDD IKLTGSAIES RICAEDPSKK FFPSSGRIRY
YNKPDENFST QLPIIPVSNT AIKEKNDWVS VSCAGVTLGS VVNLSSKQLL CKESNNCVRI
DDGVAAGSEI SMFYDSMIMK VITYGKDRIE AIGRMQKALS ECYIEGVTNN IEFLESIFHH
PNFVAAKLHT RFISDHYPNG FHGDFVTEEY VKVFIFAVLY VHLENEEKCY YKAVNETSLM
SFQRVILESR KGEELVPVSF AQMTPCGVRM TLNNIGGISN NDGTTGSRAR DLFIVRINNN
EYSINAKYQN SVLTTVYNHN TYSIIGKWKL SYRLLSITIN DDTNIILKVE KQGSRYFIRH
AGMQAECCVF KPHIARLSKF MLNNETERVA VNAVKSPISG LLVKLHVNVG DQVGVGQPLF
VVEAMKMENI ICAESEMVIK NIPVQEGKNV QVGDVVCFLK
//
