ID   PCCB_SACEN              Reviewed;         546 AA.
AC   P53003; A4FF48;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Propionyl-CoA carboxylase beta chain;
DE            Short=PCCase;
DE            EC=6.4.1.3;
DE   AltName: Full=Propanoyl-CoA:carbon dioxide ligase;
GN   Name=pccB; OrderedLocusNames=SACE_3398;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=8830278; DOI=10.1046/j.1365-2958.1996.439969.x;
RA   Donadio S., Staver M.J., Katz L.;
RT   "Erythromycin production in Saccharopolyspora erythraea does not require a
RT   functional propionyl-CoA carboxylase.";
RL   Mol. Microbiol. 19:977-984(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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   -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC       succinyl-CoA from propanoyl-CoA: step 1/3.
CC   -!- SUBUNIT: Probably a dodecamer composed of six biotin-containing alpha
CC       subunits and six beta subunits. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mutant lacks PCCase activity. Mutation has no
CC       effect on erythromycin production. {ECO:0000269|PubMed:8830278}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR   EMBL; X92557; CAA63310.1; -; Genomic_DNA.
DR   EMBL; AM420293; CAM02673.1; -; Genomic_DNA.
DR   PIR; S71008; S71008.
DR   RefSeq; WP_009949581.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; P53003; -.
DR   SMR; P53003; -.
DR   STRING; 405948.SACE_3398; -.
DR   EnsemblBacteria; CAM02673; CAM02673; SACE_3398.
DR   KEGG; sen:SACE_3398; -.
DR   eggNOG; COG4799; Bacteria.
DR   HOGENOM; CLU_018822_6_2_11; -.
DR   OMA; LDEFAQH; -.
DR   OrthoDB; 886663at2; -.
DR   UniPathway; UPA00945; UER00908.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
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   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..546
FT                   /note="Propionyl-CoA carboxylase beta chain"
FT                   /id="PRO_0000199803"
FT   DOMAIN          21..277
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          292..540
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          21..540
FT                   /note="Carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT   CONFLICT        399
FT                   /note="E -> D (in Ref. 1; CAA63310)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="G -> A (in Ref. 1; CAA63310)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   546 AA;  58526 MW;  A219DE009C9CB76E CRC64;
     MSSATEPVGV PPAEAPDIHT TAGKLADLYR RNHEAVHAGS ERAVAKQHAK GKRTARERID
     MLLDEGSFVE LDEHARHRST NFGMDADRPY GDGVVTGWGT VDGRRVCVFS QDFTVFGGSL
     GEVFGEKIVK VMDLAMKTGC PLVGINDSGG ARIQEGVAAL GLYAEIFKRN THASGVIPQI
     SLIMGPCAGG AVYSPAITDF TVMVDQTSHM FITGPDVIKT VTGEDVSFED LGGARTHNER
     SGNAHYLATD EDDAISYVKE LLSFLPSNNL SSSPVFPGAE VEEGSVADGV GDADLELDAL
     VPDSPNQPYD MREVITRLVD EGEFLEVSAL FAPNMLCGFG RIEGASVGVV ANQPMQLAGT
     LDIDASEKAA RFVRFCDAFN IPVLTLVDVP GFLPGTGQEW NGIIRRGAKL LYAYAEATVP
     LVTVITRKAY GGAYDVMGSK HLGADINLAW PTAQIAVMGA QGAANILYRR QLAEAAERGE
     DVEALRARLQ QEYEDTLCNP YVAAERGYVD SVIPPSHTRG HVARALRMLA DKREALPAKK
     HGNIPL