ID   PCCB_RHOER              Reviewed;         476 AA.
AC   Q06101;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 69.
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;
OS   Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=1833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NI86/21;
RX   PubMed=1452030; DOI=10.1016/0378-1119(92)90050-y;
RA   Nagy I., Schoofs G., Vanderleyden J., de Mot R.;
RT   "Sequence of a Rhodococcus gene encoding a protein with extensive homology
RT   to the mammalian propionyl-CoA carboxylase beta chain.";
RL   Gene 122:199-202(1992).
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.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR   EMBL; M95713; AAB80770.1; -; Genomic_DNA.
DR   PIR; JQ1943; JQ1943.
DR   AlphaFoldDB; Q06101; -.
DR   SMR; Q06101; -.
DR   STRING; 1833.XU06_17110; -.
DR   PRIDE; Q06101; -.
DR   UniPathway; UPA00945; UER00908.
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   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..476
FT                   /note="Propionyl-CoA carboxylase beta chain"
FT                   /id="PRO_0000199802"
FT   DOMAIN          1..225
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          226..476
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT   REGION          1..476
FT                   /note="Carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT   REGION          439..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   476 AA;  50450 MW;  7D1EFD1C0C77478B CRC64;
     MTILAPVTKS ESSTDPRDPL ARLENLFDPG TTVPLHARDK SGVLAASGNI DGVRTIAYCS
     DATVMGGAMG VDGCKHLVKA IDTAIEEESP IVGLWHSGGA RLAEGVEALH AVGLVFEAMV
     RASGLIPQIS VVLGFAAGGA AYGPALTDVV IMAPEGRVFV TGPDVVRSVT GEQVDMVSLG
     GPDTHTKKSG VAHIAAHDEA DALHRARRLV SMMCEQGEFD QRAAELGDSD LRAMMPASAK
     RAYDVRPIVH EMLDNVEGES SFEELQGNYA RSIVTGFGRM AGRTVGVIAN NPLRLGCLNS
     ESAEKAARFV RLCNAFGVPL VVVVDVPGYL PGVSMEWEGV VRRGAKLLHA FAEATVPRVT
     VVTRKIYGGA YIAMNSRALG ATAVFAWPNS EVAVMGAKAA VGILHKRALA AAPDDEREAL
     HDRLAAEHEA IAGGVDRRCR NRRRRRGNRP GEDSQHRHAA LASAPSVRAR HKNIPL