PCCA_MYXXA
ID PCCA_MYXXA Reviewed; 30 AA.
AC P81185;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 02-JUN-2021, entry version 77.
DE RecName: Full=Propionyl-CoA carboxylase alpha chain;
DE Short=PCCase;
DE EC=6.4.1.3 {ECO:0000269|PubMed:9683657};
DE AltName: Full=Propanoyl-CoA:carbon dioxide ligase;
DE Flags: Fragment;
OS Myxococcus xanthus.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=34;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 25232 / DSM 16526 / CIP 107069 / KCTC 72774 / NBRC 13542 /
RC NCIMB 9412 / FB;
RX PubMed=9683657; DOI=10.1007/s002030050631;
RA Kimura Y., Kojyo T., Kimura I., Sato M.;
RT "Propionyl-CoA carboxylase of Myxococcus xanthus: catalytic properties and
RT function in developing cells.";
RL Arch. Microbiol. 170:179-184(1998).
CC -!- FUNCTION: This is one of the 2 subunits of the biotin-dependent
CC propionyl-CoA carboxylase (PCC), the enzyme catalyzing the
CC carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-
CC CoA/(S)-methylmalonyl-CoA (PubMed:9683657). Within the holoenzyme, the
CC alpha subunit catalyzes the ATP-dependent carboxylation of the biotin
CC carried by the biotin carboxyl carrier (BCC) domain, while the beta
CC subunit then transfers the carboxyl group from carboxylated biotin to
CC propionyl-CoA (By similarity). Propionyl-CoA carboxylase also
CC carboxylates acetyl-CoA, butyryl-CoA and succinyl-CoA (PubMed:9683657).
CC {ECO:0000250|UniProtKB:Q5LUF3, ECO:0000269|PubMed:9683657}.
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:9683657};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23721;
CC Evidence={ECO:0000305|PubMed:9683657};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-
CC ProRule:PRU00969};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01066};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for acetyl-CoA {ECO:0000269|PubMed:9683657};
CC KM=0.2 mM for butyryl-CoA {ECO:0000269|PubMed:9683657};
CC KM=0.03 mM for propionyl-CoA {ECO:0000269|PubMed:9683657};
CC KM=1.0 mM for succinyl-CoA {ECO:0000269|PubMed:9683657};
CC pH dependence:
CC Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:9683657};
CC Temperature dependence:
CC Optimum temperature is 25-30 degrees Celsius.
CC {ECO:0000269|PubMed:9683657};
CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC succinyl-CoA from propanoyl-CoA: step 1/3.
CC {ECO:0000305|PubMed:9683657}.
CC -!- SUBUNIT: Dodecamer composed of six biotin-containing alpha subunits and
CC six beta subunits. {ECO:0000305}.
CC -!- DOMAIN: Consists of an N-terminal biotin carboxylation/carboxylase (BC)
CC domain that catalyzes the transient carboxylation of the biotin
CC covalently attached to the C-terminal biotinyl-binding/biotin carboxyl
CC carrier (BCC) domain. {ECO:0000250|UniProtKB:Q5LUF3}.
CC -!- MISCELLANEOUS: During development the activity increased gradually with
CC the maximum during the sporulation stage. {ECO:0000269|PubMed:9683657}.
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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 GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR PROSITE; PS50979; BC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Biotin; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding.
FT CHAIN 1..>30
FT /note="Propionyl-CoA carboxylase alpha chain"
FT /id="PRO_0000146818"
FT DOMAIN 1..>30
FT /note="Biotin carboxylation"
FT NON_TER 30
SQ SEQUENCE 30 AA; 3344 MW; 05D3D2827BCDDD81 CRC64;
PKIRKVLVAN RGEIAIRVMR TXKELGIATV
