P-POD: Princeton Protein Orthology Database: GO3/Nens573

This family has 30 members: 2 Arabidopsis thaliana, 3 Caenorhabditis elegans, 3 Danio rerio, 2 Dictyostelium discoideum, 2 Drosophila melanogaster, 1 Escherichia coli, 3 Gallus gallus, 3 Homo sapiens, 3 Mus musculus, 4 Rattus norvegicus, 3 Saccharomyces cerevisiae, 1 Schizosaccharomyces pombe.

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GO3/Nens573
30 members.
OrganismProtein (Synonyms)DescriptionAmiGO
A. thalianaNCBI:NP_198386.1 · TAIR:locus:2182658 (T26D22_8 · T26D22.8 · AT5G35360 · CAC2)ACETYL-COA CARBOXYLASE⌘
A. thalianaNCBI:NP_849583.1 · TAIR:locus:2007559 (MCCA · AT1G03090)⌘
C. elegansWB:WBGene00017864 (F27D9.5 · pcca-1) · UniProtKB:Q19842⌘
C. elegansWB:WBGene00004258 (D2023.2 · pyc-1) · UniProtKB:O17732⌘
C. elegansWB:WBGene00009319 (F32B6.2) · UniProtKB:O45430⌘
D. rerioUniProtKB:Q6DGE2 · ZFIN:ZDB-GENE-040718-246 (pcca)propionyl-Coenzyme A carboxylase, alpha polypeptide⌘
D. rerioZFIN:ZDB-GENE-061103-95 (zgc:154106) · UniProtKB:A0JMP7⌘
D. rerioUniProtKB:B3DGZ9 · ZFIN:ZDB-GENE-000831-1 (pc)pyruvate carboxylase⌘
D. discoideumUniProtKB:Q54KE6 · dictyBase:DDB_G0287377 (mccA · MCCC1)methylcrotonyl-CoA carboxylase, 3-methylcrotonyl-CoA:carbon dioxide ligase alpha subunit⌘
D. discoideumUniProtKB:Q553S7 · dictyBase:DDB_G0275355 (pccA)propionyl-CoA carboxylase, propanoyl-CoA:carbon dioxide ligase alpha subunit⌘
D. melanogasterUniProtKB:Q0E9E2 · FB:FBgn0027580 (BcDNA · BcDNA:GH06348 · CG1516 · GH06348 · PC)pyruvate carboxylase⌘
D. melanogasterUniProtKB:Q9V9T5 · FB:FBgn0039877 (CG2118 · MCC · mcc)3-methyl-crotonyl-CoA carboxylase⌘
E. coliUniProtKB:P24182 · ECOLI:BIOTIN-CARBOXYL-MONOMER (fabG · accC · AccC · ECK3243 · b3256)⌘
G. gallusNCBI:XP_416970 · ENTREZ:418774
G. gallusUniProtKB:Q5ZK45 (RCJMB04_13e11 · IPI00583497 · Q5ZK45) · ENTREZ:424962⌘
G. gallusUniProtKB:Q8JHF6 (PYC · Q8JHF6 · IPI00580024) · ENTREZ:374263⌘
H. sapiensENSEMBL:ENSG00000078070 · UniProtKB:Q96RQ3 (MCCA_HUMAN · IPI00024580 · MCCA · Q96RQ3 · MCCC1)Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial⌘
H. sapiensENSEMBL:ENSG00000175198 · UniProtKB:P05165 (PCCA_HUMAN · PCCA · IPI00744115 · P05165)Propionyl-CoA carboxylase alpha chain, mitochondrial⌘
H. sapiensENSEMBL:ENSG00000173599 · UniProtKB:P11498 (P11498 · PYC_HUMAN · IPI00299402 · PC)Pyruvate carboxylase, mitochondrial⌘
M. musculusUniProtKB:Q99MR8 · MGI:MGI:1919289 (MCCalpha · Mccc1 · MCCA)methylcrotonoyl-Coenzyme A carboxylase 1 (alpha)⌘
M. musculusUniProtKB:Q91ZA3 · MGI:MGI:97499 (C79630 · Pcca)propionyl-Coenzyme A carboxylase, alpha polypeptide⌘
M. musculusUniProtKB:Q05920 · MGI:MGI:97520 (Pcx · Pc)pyruvate carboxylase⌘
R. norvegicusRGD:1590160 · NCBI:XP_001075496
R. norvegicusUniProtKB:P14882 · RGD:3264 (Pcca)propionyl-coenzyme A carboxylase, alpha polypeptide⌘
R. norvegicusUniProtKB:P52873 · RGD:3262 (Pc)pyruvate carboxylase⌘
R. norvegicusUniProtKB:Q5I0C3 · RGD:1310615 (Mccc1)methylcrotonoyl-Coenzyme A carboxylase 1 (alpha)⌘
S. cerevisiaeUniProtKB:P32528 · SGD:S000000412 (DUR80 · YBR208C · DUR1,2)Urea amidolyase, contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3⌘
S. cerevisiaeUniProtKB:P11154 · SGD:S000003030 (YGL062W · PYC1)Pyruvate carboxylase isoform, cytoplasmic enzyme that converts pyruvate to oxaloacetate⌘
S. cerevisiaeUniProtKB:P32327 · SGD:S000000422 (YBR218C · PYC2)Pyruvate carboxylase isoform, cytoplasmic enzyme that converts pyruvate to oxaloacetate⌘
S. pombeUniProtKB:Q9UUE1 · GeneDB_Spombe:SPBC17G9.11c (pyr1 · SPBC17G9.11c)pyruvate carboxylase⌘
ProteinPublicationCurator Notes
UniProtKB:P32327 · SGD:S000000422PMID:10481094 Bauer J, et al. By-product formation during exposure of respiring Saccharomyces cerevisiae cultures to excess glucose is not caused by a limited capacity of pyruvate carboxylase. FEMS Microbiol Lett. 1999 Oct 1;179(1):107-13.The E. coli protein Phosphoenolpyruvate carboxylase complements a homologous mutation in S. cerevisiae.
UniProtKB:P11154 · SGD:S000003030PMID:10481094 Bauer J, et al. By-product formation during exposure of respiring Saccharomyces cerevisiae cultures to excess glucose is not caused by a limited capacity of pyruvate carboxylase. FEMS Microbiol Lett. 1999 Oct 1;179(1):107-13.The E. coli protein Phosphoenolpyruvate carboxylase complements a homologous mutation in S. cerevisiae.
UniProtKB:P32327 · SGD:S000000422PMID:15701798 Flores CL, et al. Yarrowia lipolytica mutants devoid of pyruvate carboxylase activity show an unusual growth phenotype. Eukaryot Cell. 2005 Feb;4(2):356-64.The Y. lipolytica protein PYC1 complements a homologous mutation in S. cerevisiae. The Y. lipolytica PYC1 gene complemented the growth defect of a Saccharomyces cerevisiae pyc1 pyc2 mutant.
UniProtKB:P11154 · SGD:S000003030PMID:15701798 Flores CL, et al. Yarrowia lipolytica mutants devoid of pyruvate carboxylase activity show an unusual growth phenotype. Eukaryot Cell. 2005 Feb;4(2):356-64.The Y. lipolytica protein PYC1 complements a homologous mutation in S. cerevisiae. The Y. lipolytica PYC1 gene complemented the growth defect of a Saccharomyces cerevisiae pyc1 pyc2 mutant.
DescriptionSuffix
Sequences in this family.fasta
mafft aligned Fasta file.afasta
phyml newick file.newick
Notung rooted & rearranged newick file.newick.rooting.0.rearrange.0
Notung Homolog Table.newick.rooting.0.rearrange.0.homologs.csv
OMIM (3)
ENSEMBL:ENSG00000175198 · UniProtKB:P05165#210200 3-@METHYLCROTONYL-CoA CARBOXYLASE 1 DEFICIENCY;;MCCD TYPE 1;;MCC1 DEFICIENCY;;3-@METHYLCROTONYLGLYCINURIA I;;METHYLCROTONYLGLYCINURIA TYPE I
ENSEMBL:ENSG00000173599 · UniProtKB:P11498#606054 PROPIONIC ACIDEMIA;;PROPIONYL-CoA CARBOXYLASE DEFICIENCY;;PCC DEFICIENCY;;GLYCINEMIA, KETOTIC;;HYPERGLYCINEMIA WITH KETOACIDOSIS AND LEUKOPENIA;;KETOTIC HYPERGLYCINEMIA
UniProtKB:P11154 · SGD:S000003030#266150 PYRUVATE CARBOXYLASE DEFICIENCY;;PC DEFICIENCY;;ATAXIA WITH LACTIC ACIDOSIS II;;LEIGH NECROTIZING ENCEPHALOPATHY DUE TO PYRUVATE CARBOXYLASE DEFICIENCY;;LEIGH SYNDROME DUE TO PYRUVATE CARBOXYLASE DEFICIENCY
SGD Disease Papers (1)
UniProtKB:P11154 · SGD:S000003030PMID:9300813 Foury F (1997) Human genetic diseases: a cross-talk between man and yeast. Gene 195(1):1-10
Send questions, suggestions, and comments to: yfgdb@genomics.princeton.edu