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Protein

Pyruvate carboxylase

Gene

pyr1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.By similarity

Catalytic activityi

ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: gluconeogenesis

This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei150ATPBy similarity1
Binding sitei234ATPBy similarity1
Binding sitei269ATPBy similarity1
Active sitei326By similarity1
Metal bindingi579Divalent metal cationBy similarity1
Binding sitei651SubstrateBy similarity1
Metal bindingi747Divalent metal cation; via carbamate groupBy similarity1
Metal bindingi777Divalent metal cationBy similarity1
Metal bindingi779Divalent metal cationBy similarity1
Binding sitei912SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Gluconeogenesis

Keywords - Ligandi

ATP-binding, Biotin, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-196780. Biotin transport and metabolism.
R-SPO-70263. Gluconeogenesis.
UniPathwayiUPA00138.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate carboxylase (EC:6.4.1.1)
Alternative name(s):
Pyruvic carboxylase
Short name:
PCB
Gene namesi
Name:pyr1
ORF Names:SPBC17G9.11c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC17G9.11c.
PomBaseiSPBC17G9.11c. pyr1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001468231 – 1185Pyruvate carboxylaseAdd BLAST1185

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei747N6-carboxylysineBy similarity1
Modified residuei1149N6-biotinyllysinePROSITE-ProRule annotationBy similarity1

Proteomic databases

MaxQBiQ9UUE1.
PRIDEiQ9UUE1.

Interactioni

Protein-protein interaction databases

MINTiMINT-4712482.

Structurei

3D structure databases

ProteinModelPortaliQ9UUE1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 484Biotin carboxylationAdd BLAST453
Domaini154 – 351ATP-graspPROSITE-ProRule annotationAdd BLAST198
Domaini570 – 838Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST269
Domaini1108 – 1183Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST76

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni578 – 582Substrate bindingBy similarity5

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.Curated
Contains 1 biotinyl-binding domain.PROSITE-ProRule annotationCurated
Contains 1 pyruvate carboxyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000282801.
InParanoidiQ9UUE1.
KOiK01958.
OMAiYYLDFVD.
OrthoDBiEOG092C0BFY.
PhylomeDBiQ9UUE1.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.20.20.70. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR003379. Carboxylase_cons_dom.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR009057. Homeodomain-like.
IPR016185. PreATP-grasp_dom.
IPR000891. PYR_CT.
IPR005930. Pyruv_COase.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. Biotin_carb_N. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PIRSFiPIRSF001594. Pyruv_carbox. 1 hit.
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01235. pyruv_carbox. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00867. CPSASE_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UUE1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSKYDALLH NQSTNTNPFS KLQDRSSLLG EKFTKVLVAN RSEIAIRVFR
60 70 80 90 100
TAHELSMHTV AIYSYEDRLS MHRQKADESY PIGKVGQYSP VGAYLAIDEI
110 120 130 140 150
VSIAKRTGAN LVHPGYGFLS ENAEFARKVN EAGMQFVGPS PEVIDSLGDK
160 170 180 190 200
TKARAIAIRC GVPVVPGTPG PVEHYEEAEA FVKEYGLPVI IKAAMGGGGR
210 220 230 240 250
GMRVVRSADT LKESFERARS EALASFGDGT VFIERFLDKP KHIEIQLMAD
260 270 280 290 300
KAGNVIHLHE RDCSVQRRHQ KVVEIAPAKD LDPKIRQALY DDAIKIAKEV
310 320 330 340 350
KYCNAGTAEF LLDQKGRHYF IEINPRIQVE HTITEEITGV DIVSAQLHVA
360 370 380 390 400
AGFTLPEIGL TQDKISTRGF AIQCRVTTED PNNGFAPDIG KIEVYRSAGG
410 420 430 440 450
NGVRLDGANG FAGSVITPHY DSMLVKCTCH DATYEYTRRK MIRSLIEFRV
460 470 480 490 500
RGVKTNIPFV LRLLMHDTFI QGNCWTTFID DTPELFQLYR SRNRAQKLLA
510 520 530 540 550
YLGDLAVNGS SIKGQNGEPA LKSEIVMPVL LDSTGNQIDV SHPSEKGWRK
560 570 580 590 600
LLLDNGPAAF AKAVRNHKRG LIMDTTWRDA HQSLLATRVR TIDLVNIAPY
610 620 630 640 650
TSHALASAYS LEMWGGATFD VSMRFLHECP WDRLRRLRKL VPNIPFQMLL
660 670 680 690 700
RGANGLCYSS LPDNVIYFFC EQAKKNGIDI FRVFDALNDV NNLSLGIDAA
710 720 730 740 750
KRAGGVVEAT MCYSGDMLNP KKKYNLDYYV NLVDKMVEMG IHILGIKDMA
760 770 780 790 800
GVMKPKAARL LISAIREKHP ELPIHVHTHD SAGTAVASMA AALEAGADVV
810 820 830 840 850
DVATDSMSGL TSQPSFGAVL ASVDGTDKQL EFDNNQLREI DSYWAQMRLL
860 870 880 890 900
YSPFESEIKG TDSDVYNHEI PGGQLTNLKF QATSLGLGTQ WAETKKAYIE
910 920 930 940 950
ANKLLGDIIK VTPTSKVVGD LAQFMVQNKL SAEDVENRAT TLDFPASVLD
960 970 980 990 1000
FFQGLMGQPY GGFPEPLRTN VLKGRRQPLT DRPGKFLPAA DFDAIRKLLS
1010 1020 1030 1040 1050
EKFGVSSDCD IAAYTQFPGV FEEYRQFVDR YGDLTTVPTK FFLSRPEMNE
1060 1070 1080 1090 1100
EMHVEIDQGK TLIVKFVALG PLNPRTGQRE VYFELNGENR HVTVEDKKAA
1110 1120 1130 1140 1150
IETVTRPRAD PGNPGHVAAP MSGTIVEIRV KEGAKVKKGD IIAVLSAMKM
1160 1170 1180
EIVISAPHSG VLKSLAVVQG DSVNGGDLCA VLEHE
Length:1,185
Mass (Da):130,861
Last modified:May 1, 2000 - v1
Checksum:iD39706DCD83915D9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti68R → I in BAA11239 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78170 Genomic DNA. Translation: BAA11239.1.
CU329671 Genomic DNA. Translation: CAB52809.1.
PIRiT39734.
RefSeqiNP_595900.1. NM_001021807.2.

Genome annotation databases

EnsemblFungiiSPBC17G9.11c.1; SPBC17G9.11c.1:pep; SPBC17G9.11c.
GeneIDi2539661.
KEGGispo:SPBC17G9.11c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78170 Genomic DNA. Translation: BAA11239.1.
CU329671 Genomic DNA. Translation: CAB52809.1.
PIRiT39734.
RefSeqiNP_595900.1. NM_001021807.2.

3D structure databases

ProteinModelPortaliQ9UUE1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4712482.

Proteomic databases

MaxQBiQ9UUE1.
PRIDEiQ9UUE1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC17G9.11c.1; SPBC17G9.11c.1:pep; SPBC17G9.11c.
GeneIDi2539661.
KEGGispo:SPBC17G9.11c.

Organism-specific databases

EuPathDBiFungiDB:SPBC17G9.11c.
PomBaseiSPBC17G9.11c. pyr1.

Phylogenomic databases

HOGENOMiHOG000282801.
InParanoidiQ9UUE1.
KOiK01958.
OMAiYYLDFVD.
OrthoDBiEOG092C0BFY.
PhylomeDBiQ9UUE1.

Enzyme and pathway databases

UniPathwayiUPA00138.
ReactomeiR-SPO-196780. Biotin transport and metabolism.
R-SPO-70263. Gluconeogenesis.

Miscellaneous databases

PROiQ9UUE1.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.20.20.70. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR003379. Carboxylase_cons_dom.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR009057. Homeodomain-like.
IPR016185. PreATP-grasp_dom.
IPR000891. PYR_CT.
IPR005930. Pyruv_COase.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. Biotin_carb_N. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
PIRSFiPIRSF001594. Pyruv_carbox. 1 hit.
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR01235. pyruv_carbox. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00867. CPSASE_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPYC_SCHPO
AccessioniPrimary (citable) accession number: Q9UUE1
Secondary accession number(s): P78822
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.