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Protein

Propionyl-CoA carboxylase beta chain, mitochondrial

Gene

Pccb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA.

Pathwayi: propanoyl-CoA degradation

This protein is involved in step 1 of the subpathway that synthesizes succinyl-CoA from propanoyl-CoA.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Propionyl-CoA carboxylase alpha chain, mitochondrial (Pcca), Propionyl-CoA carboxylase beta chain, mitochondrial (Pccb)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway propanoyl-CoA degradation, which is itself part of Metabolic intermediate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinyl-CoA from propanoyl-CoA, the pathway propanoyl-CoA degradation and in Metabolic intermediate metabolism.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • propionyl-CoA carboxylase activity Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.4.1.3. 3474.
ReactomeiR-MMU-196780. Biotin transport and metabolism.
R-MMU-71032. Propionyl-CoA catabolism.
UniPathwayiUPA00945; UER00908.

Names & Taxonomyi

Protein namesi
Recommended name:
Propionyl-CoA carboxylase beta chain, mitochondrial (EC:6.4.1.3)
Short name:
PCCase subunit beta
Alternative name(s):
Propanoyl-CoA:carbon dioxide ligase subunit beta
Gene namesi
Name:Pccb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1914154. Pccb.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionBy similarityAdd
BLAST
Chaini29 – 541513Propionyl-CoA carboxylase beta chain, mitochondrialPRO_0000000294Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei73 – 731PhosphoserineBy similarity
Modified residuei101 – 1011N6-acetyllysine; alternateCombined sources
Modified residuei101 – 1011N6-succinyllysine; alternateCombined sources
Modified residuei250 – 2501N6-succinyllysineCombined sources
Modified residuei476 – 4761N6-acetyllysine; alternateCombined sources
Modified residuei476 – 4761N6-succinyllysine; alternateCombined sources
Modified residuei491 – 4911N6-acetyllysine; alternateCombined sources
Modified residuei491 – 4911N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ99MN9.
MaxQBiQ99MN9.
PaxDbiQ99MN9.
PRIDEiQ99MN9.

2D gel databases

REPRODUCTION-2DPAGEQ99MN9.

PTM databases

iPTMnetiQ99MN9.
PhosphoSiteiQ99MN9.
SwissPalmiQ99MN9.

Expressioni

Tissue specificityi

Broadly expressed. Most abundantly expressed in the kidney, liver, small intestine and stomach.1 Publication

Gene expression databases

BgeeiQ99MN9.
ExpressionAtlasiQ99MN9. baseline and differential.
GenevisibleiQ99MN9. MM.

Interactioni

Subunit structurei

Probably a dodecamer composed of six biotin-containing alpha subunits and six beta subunits.By similarity

Protein-protein interaction databases

IntActiQ99MN9. 2 interactions.
MINTiMINT-1861971.
STRINGi10090.ENSMUSP00000035116.

Structurei

3D structure databases

ProteinModelPortaliQ99MN9.
SMRiQ99MN9. Positions 39-541.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 533494CarboxyltransferaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni327 – 36034Acyl-CoA bindingSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the AccD/PCCB family.Curated
Contains 1 carboxyltransferase domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0540. Eukaryota.
COG4799. LUCA.
GeneTreeiENSGT00530000063337.
HOGENOMiHOG000218693.
HOVERGENiHBG003970.
InParanoidiQ99MN9.
KOiK01966.
OMAiFEEYDMY.
OrthoDBiEOG7353WZ.
TreeFamiTF314350.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99MN9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAIRIRAV AAGARLSVLN CGLGITTRGL CSQPVSVKER IDNKRHAALL
60 70 80 90 100
GGGQRRIDAQ HKRGKLTARE RISLLLDPGS FMESDMFVEH RCADFGMAAD
110 120 130 140 150
KNKFPGDSVV TGRGRINGRL VYVFSQDFTV FGGSLSGAHA QKICKIMDQA
160 170 180 190 200
ITVGAPVIGL NDSGGARIQE GVESLAGYAD IFLRNVTASG VIPQISLIMG
210 220 230 240 250
PCAGGAVYSP ALTDFTFMVK DTSYLFITGP EVVKSVTNED VTQEQLGGAK
260 270 280 290 300
THTTVSGVAH RAFDNDVDAL CNLREFFNFL PLSSQDPAPI RECHDPSDRL
310 320 330 340 350
VPELDTVVPL ESSKAYNMLD IIHAVIDERE FFEIMPSYAK NIVVGFARMN
360 370 380 390 400
GRTVGIVGNQ PNVASGCLDI NSSVKGARFV RFCDAFNIPL ITFVDVPGFL
410 420 430 440 450
PGTAQEYGGI IRHGAKLLYA FAEATVPKIT VITRKAYGGA YDVMSSKHLL
460 470 480 490 500
GDTNYAWPTA EIAVMGAKGA VEIIFKGHQD VEAAQAEYVE KFANPFPAAV
510 520 530 540
RGFVDDIIQP SSTRARICCD LEVLASKKVH RPWRKHANIP L
Length:541
Mass (Da):58,409
Last modified:July 27, 2011 - v2
Checksum:i1DFB5978BD81103B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti340 – 3401K → L in AAK28525 (PubMed:11245989).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF327060 mRNA. Translation: AAK28525.1.
AK004976 mRNA. Translation: BAB23712.1.
AK050366 mRNA. Translation: BAC34211.1.
CCDSiCCDS23442.1.
RefSeqiNP_001298078.1. NM_001311149.1.
NP_080111.1. NM_025835.3.
UniGeneiMm.335385.

Genome annotation databases

EnsembliENSMUST00000035116; ENSMUSP00000035116; ENSMUSG00000032527.
GeneIDi66904.
KEGGimmu:66904.
UCSCiuc009rfc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF327060 mRNA. Translation: AAK28525.1.
AK004976 mRNA. Translation: BAB23712.1.
AK050366 mRNA. Translation: BAC34211.1.
CCDSiCCDS23442.1.
RefSeqiNP_001298078.1. NM_001311149.1.
NP_080111.1. NM_025835.3.
UniGeneiMm.335385.

3D structure databases

ProteinModelPortaliQ99MN9.
SMRiQ99MN9. Positions 39-541.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99MN9. 2 interactions.
MINTiMINT-1861971.
STRINGi10090.ENSMUSP00000035116.

PTM databases

iPTMnetiQ99MN9.
PhosphoSiteiQ99MN9.
SwissPalmiQ99MN9.

2D gel databases

REPRODUCTION-2DPAGEQ99MN9.

Proteomic databases

EPDiQ99MN9.
MaxQBiQ99MN9.
PaxDbiQ99MN9.
PRIDEiQ99MN9.

Protocols and materials databases

DNASUi66904.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035116; ENSMUSP00000035116; ENSMUSG00000032527.
GeneIDi66904.
KEGGimmu:66904.
UCSCiuc009rfc.1. mouse.

Organism-specific databases

CTDi5096.
MGIiMGI:1914154. Pccb.

Phylogenomic databases

eggNOGiKOG0540. Eukaryota.
COG4799. LUCA.
GeneTreeiENSGT00530000063337.
HOGENOMiHOG000218693.
HOVERGENiHBG003970.
InParanoidiQ99MN9.
KOiK01966.
OMAiFEEYDMY.
OrthoDBiEOG7353WZ.
TreeFamiTF314350.

Enzyme and pathway databases

UniPathwayiUPA00945; UER00908.
BRENDAi6.4.1.3. 3474.
ReactomeiR-MMU-196780. Biotin transport and metabolism.
R-MMU-71032. Propionyl-CoA catabolism.

Miscellaneous databases

ChiTaRSiPccb. mouse.
PROiQ99MN9.
SOURCEiSearch...

Gene expression databases

BgeeiQ99MN9.
ExpressionAtlasiQ99MN9. baseline and differential.
GenevisibleiQ99MN9. MM.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning, mapping and expression of the mouse propionyl CoA carboxylase beta (pccb), the gene for human type II propionic acidaemia."
    Schrick J.J., Lingrel J.B.
    Gene 264:147-152(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Kidney.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-101; LYS-250; LYS-476 AND LYS-491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101; LYS-476 AND LYS-491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPCCB_MOUSE
AccessioniPrimary (citable) accession number: Q99MN9
Secondary accession number(s): Q9DBG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.