PCCB_CERS4
ID PCCB_CERS4 Reviewed; 510 AA.
AC Q3J4E3;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Propionyl-CoA carboxylase beta chain {ECO:0000305};
DE Short=PCCase {ECO:0000305};
DE EC=6.4.1.3 {ECO:0000269|PubMed:26170412};
DE AltName: Full=Propanoyl-CoA:carbon dioxide ligase {ECO:0000305};
GN Name=pccB {ECO:0000303|PubMed:26170412};
GN OrderedLocusNames=RHOS4_07730 {ECO:0000305};
GN ORFNames=RSP_2189 {ECO:0000312|EMBL:ABA78341.1};
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1. {ECO:0000312|Proteomes:UP000002703};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP CATALYTIC ACTIVITY, PATHWAY, AND INDUCTION.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RX PubMed=26170412; DOI=10.1128/jb.00402-15;
RA Carter M.S., Alber B.E.;
RT "Transcriptional regulation by the short-chain fatty acyl coenzyme A
RT regulator (ScfR) PccR controls propionyl coenzyme A assimilation by
RT Rhodobacter sphaeroides.";
RL J. Bacteriol. 197:3048-3056(2015).
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:0000269|PubMed:26170412};
CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC succinyl-CoA from propanoyl-CoA: step 1/3.
CC {ECO:0000305|PubMed:26170412}.
CC -!- SUBUNIT: Probably a dodecamer composed of six biotin-containing alpha
CC subunits and six beta subunits. {ECO:0000250}.
CC -!- INDUCTION: Transcriptionally regulated by PccR. Expression is dependent
CC on the carbon source supplied: transcript levels from acetate- and
CC propionate-grown cells increase 6- and 10-fold, respectively, when
CC compared with succinate-grown cells. {ECO:0000269|PubMed:26170412}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR EMBL; CP000143; ABA78341.1; -; Genomic_DNA.
DR RefSeq; WP_002719342.1; NZ_CP030271.1.
DR RefSeq; YP_352242.1; NC_007493.2.
DR AlphaFoldDB; Q3J4E3; -.
DR SMR; Q3J4E3; -.
DR STRING; 272943.RSP_2189; -.
DR EnsemblBacteria; ABA78341; ABA78341; RSP_2189.
DR GeneID; 57469543; -.
DR KEGG; rsp:RSP_2189; -.
DR PATRIC; fig|272943.9.peg.1085; -.
DR eggNOG; COG4799; Bacteria.
DR OMA; PQNNREN; -.
DR PhylomeDB; Q3J4E3; -.
DR BioCyc; MetaCyc:MON-13590; -.
DR UniPathway; UPA00945; UER00908.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..510
FT /note="Propionyl-CoA carboxylase beta chain"
FT /id="PRO_0000434654"
FT DOMAIN 1..257
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 264..504
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 1..504
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
SQ SEQUENCE 510 AA; 56122 MW; A4EE9432CFF224EC CRC64;
MKDILQELEN RRAIARAGGG QRRVEAQHKR GKLTARERIE LLLDEGSFEE FDMFVRHRCT
DFGMQDDRPA GDGVVTGWGT INGRMVYVFS QDFTVFGGSL SETHAQKICK IMDMAMQNGA
PVIGLNDSGG ARIQEGVASL AGYADVFQRN IMASGVIPQI SVIMGPCAGG AVYSPAMTDF
IFMVRDTSYM FVTGPDVVKT VTNEVVTAEE LGGASTHTKK SSVADGAFEN DVEALYEIRR
LVDFLPLSNR TPAPVRPFFD DVARIEDSLD TLIPDNPNQP YDMKELILKI ADEADFYEIQ
KDFAANIITG FIRLEGQTVG VVANQPMVLA GCLDIDSSRK AARFVRFCDA FNIPILTLVD
VPGFLPGTGQ EYGGVIKHGA KLLFAYGEAT VPKVTVITRK AYGGAYDVMA SKHLRGDFNY
AWPTAEIAVM GAKGATEILY RSELGDKEKI AARAKEYEDR FANPFVAAER GFIDEVIMPH
STRRRVSKAF ASLRNKKLAN PWKKHDNIPL
