PCCB_MOUSE
ID PCCB_MOUSE Reviewed; 541 AA.
AC Q99MN9; Q9DBG2;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Propionyl-CoA carboxylase beta chain, mitochondrial {ECO:0000305|PubMed:11245989};
DE Short=PCCase subunit beta;
DE EC=6.4.1.3 {ECO:0000250|UniProtKB:P05166};
DE AltName: Full=Propanoyl-CoA:carbon dioxide ligase subunit beta;
DE Flags: Precursor;
GN Name=Pccb {ECO:0000312|MGI:MGI:1914154};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=11245989; DOI=10.1016/s0378-1119(00)00586-2;
RA Schrick J.J., Lingrel J.B.;
RT "cDNA cloning, mapping and expression of the mouse propionyl CoA
RT carboxylase beta (pccb), the gene for human type II propionic acidaemia.";
RL Gene 264:147-152(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-101; LYS-250; LYS-476 AND
RP LYS-491, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101; LYS-476 AND LYS-491, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: This is one of the 2 subunits of the biotin-dependent
CC propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the
CC catabolism of odd chain fatty acids, branched-chain amino acids
CC isoleucine, threonine, methionine, and valine and other metabolites.
CC Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-
CC CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (By
CC similarity). Within the holoenzyme, the alpha subunit catalyzes the
CC ATP-dependent carboxylation of the biotin carried by the biotin
CC carboxyl carrier (BCC) domain, while the beta subunit then transfers
CC the carboxyl group from carboxylated biotin to propionyl-CoA (By
CC similarity). Propionyl-CoA carboxylase also significantly acts on
CC butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-
CC ethylmalonyl-CoA (By similarity). Other alternative minor substrates
CC include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity).
CC {ECO:0000250|UniProtKB:P05166, ECO:0000250|UniProtKB:P79384,
CC ECO:0000250|UniProtKB:Q168G2}.
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:0000250|UniProtKB:P05166};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23721;
CC Evidence={ECO:0000250|UniProtKB:P05166};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + butanoyl-CoA + hydrogencarbonate = (2S)-ethylmalonyl-CoA
CC + ADP + H(+) + phosphate; Xref=Rhea:RHEA:59520, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:60909, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P79384};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59521;
CC Evidence={ECO:0000250|UniProtKB:P79384};
CC -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA degradation;
CC succinyl-CoA from propanoyl-CoA: step 1/3.
CC {ECO:0000250|UniProtKB:P05166}.
CC -!- SUBUNIT: The holoenzyme is a dodecamer composed of 6 PCCA/alpha
CC subunits and 6 PCCB/beta subunits. {ECO:0000250|UniProtKB:P05166}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P05166}.
CC -!- TISSUE SPECIFICITY: Broadly expressed. Most abundantly expressed in the
CC kidney, liver, small intestine and stomach.
CC {ECO:0000269|PubMed:11245989}.
CC -!- DOMAIN: The beta subunit contains the carboxyl transferase (CT) domain.
CC {ECO:0000250|UniProtKB:Q168G2}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR EMBL; AF327060; AAK28525.1; -; mRNA.
DR EMBL; AK004976; BAB23712.1; -; mRNA.
DR EMBL; AK050366; BAC34211.1; -; mRNA.
DR CCDS; CCDS23442.1; -.
DR RefSeq; NP_001298078.1; NM_001311149.1.
DR RefSeq; NP_080111.1; NM_025835.3.
DR AlphaFoldDB; Q99MN9; -.
DR SMR; Q99MN9; -.
DR BioGRID; 211800; 6.
DR IntAct; Q99MN9; 2.
DR MINT; Q99MN9; -.
DR STRING; 10090.ENSMUSP00000035116; -.
DR iPTMnet; Q99MN9; -.
DR PhosphoSitePlus; Q99MN9; -.
DR SwissPalm; Q99MN9; -.
DR REPRODUCTION-2DPAGE; Q99MN9; -.
DR EPD; Q99MN9; -.
DR jPOST; Q99MN9; -.
DR MaxQB; Q99MN9; -.
DR PaxDb; Q99MN9; -.
DR PeptideAtlas; Q99MN9; -.
DR PRIDE; Q99MN9; -.
DR ProteomicsDB; 287964; -.
DR Antibodypedia; 33408; 217 antibodies from 30 providers.
DR DNASU; 66904; -.
DR Ensembl; ENSMUST00000035116; ENSMUSP00000035116; ENSMUSG00000032527.
DR GeneID; 66904; -.
DR KEGG; mmu:66904; -.
DR UCSC; uc009rfc.1; mouse.
DR CTD; 5096; -.
DR MGI; MGI:1914154; Pccb.
DR VEuPathDB; HostDB:ENSMUSG00000032527; -.
DR eggNOG; KOG0540; Eukaryota.
DR GeneTree; ENSGT00940000157741; -.
DR HOGENOM; CLU_018822_6_0_1; -.
DR InParanoid; Q99MN9; -.
DR OMA; YAYAECT; -.
DR OrthoDB; 402617at2759; -.
DR PhylomeDB; Q99MN9; -.
DR TreeFam; TF314350; -.
DR BRENDA; 6.4.1.3; 3474.
DR Reactome; R-MMU-196780; Biotin transport and metabolism.
DR Reactome; R-MMU-71032; Propionyl-CoA catabolism.
DR UniPathway; UPA00945; UER00908.
DR BioGRID-ORCS; 66904; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pccb; mouse.
DR PRO; PR:Q99MN9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q99MN9; protein.
DR Bgee; ENSMUSG00000032527; Expressed in brown adipose tissue and 246 other tissues.
DR ExpressionAtlas; Q99MN9; baseline and differential.
DR Genevisible; Q99MN9; MM.
DR GO; GO:1902494; C:catalytic complex; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; ISS:UniProtKB.
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 Acetylation; ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 29..541
FT /note="Propionyl-CoA carboxylase beta chain, mitochondrial"
FT /id="PRO_0000000294"
FT DOMAIN 34..292
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 296..535
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 34..535
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 327..360
FT /note="Acyl-CoA binding"
FT /evidence="ECO:0000255"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05166"
FT MOD_RES 101
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 101
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 250
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 476
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 476
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 491
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 491
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 340
FT /note="K -> L (in Ref. 1; AAK28525)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 58409 MW; 1DFB5978BD81103B CRC64;
MAAAIRIRAV AAGARLSVLN CGLGITTRGL CSQPVSVKER IDNKRHAALL GGGQRRIDAQ
HKRGKLTARE RISLLLDPGS FMESDMFVEH RCADFGMAAD KNKFPGDSVV TGRGRINGRL
VYVFSQDFTV FGGSLSGAHA QKICKIMDQA ITVGAPVIGL NDSGGARIQE GVESLAGYAD
IFLRNVTASG VIPQISLIMG PCAGGAVYSP ALTDFTFMVK DTSYLFITGP EVVKSVTNED
VTQEQLGGAK THTTVSGVAH RAFDNDVDAL CNLREFFNFL PLSSQDPAPI RECHDPSDRL
VPELDTVVPL ESSKAYNMLD IIHAVIDERE FFEIMPSYAK NIVVGFARMN GRTVGIVGNQ
PNVASGCLDI NSSVKGARFV RFCDAFNIPL ITFVDVPGFL PGTAQEYGGI IRHGAKLLYA
FAEATVPKIT VITRKAYGGA YDVMSSKHLL GDTNYAWPTA EIAVMGAKGA VEIIFKGHQD
VEAAQAEYVE KFANPFPAAV RGFVDDIIQP SSTRARICCD LEVLASKKVH RPWRKHANIP
L
