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Q9RNU9

- CAPP_STRCO

UniProt

Q9RNU9 - CAPP_STRCO

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Protein

Phosphoenolpyruvate carboxylase

Gene

ppc

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.UniRule annotation

Catalytic activityi

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.UniRule annotation

Cofactori

Magnesium.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei137 – 1371UniRule annotation
Active sitei569 – 5691UniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. phosphoenolpyruvate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. carbon fixation Source: UniProtKB-HAMAP
  2. oxaloacetate metabolic process Source: UniProtKB-HAMAP
  3. tricarboxylic acid cycle Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbon dioxide fixation

Keywords - Ligandi

Magnesium

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate carboxylaseUniRule annotation (EC:4.1.1.31UniRule annotation)
Short name:
PEPCUniRule annotation
Short name:
PEPCaseUniRule annotation
Gene namesi
Name:ppcUniRule annotation
Ordered Locus Names:SCO3127
ORF Names:SCE66.06c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
ProteomesiUP000001973: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 911911Phosphoenolpyruvate carboxylasePRO_0000166628Add
BLAST

Proteomic databases

PRIDEiQ9RNU9.

Interactioni

Protein-protein interaction databases

STRINGi100226.SCO3127.

Structurei

3D structure databases

ProteinModelPortaliQ9RNU9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PEPCase type 1 family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2352.
HOGENOMiHOG000238647.
InParanoidiQ9RNU9.
KOiK01595.
OMAiELSTISC.
OrthoDBiEOG6TJ7T8.
PhylomeDBiQ9RNU9.

Family and domain databases

HAMAPiMF_00595. PEPcase_type1.
InterProiIPR021135. PEP_COase.
IPR018129. PEP_COase_AS.
IPR022805. PEP_COase_bac/pln-type.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF00311. PEPcase. 1 hit.
[Graphical view]
PRINTSiPR00150. PEPCARBXLASE.
SUPFAMiSSF51621. SSF51621. 1 hit.
PROSITEiPS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9RNU9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSADDQTTT TTSSELRADI RRLGDLLGET LVRQEGPELL ELVEKVRRLT
60 70 80 90 100
REDGEAAAEL LRGTELETAA KLVRAFSTYF HLANVTEQVH RGRELGAKRA
110 120 130 140 150
AEGGLLARTA DRLKDADPEH LRETVRNLNV RPVFTAHPTE AARRSVLNKL
160 170 180 190 200
RRIAALLDTP VNESDRRRLD TRLAENIDLV WQTDELRVVR PEPADEARNA
210 220 230 240 250
IYYLDELHLG AVGDVLEDLT AELERAGVKL PDDTRPLTFG TWIGGDRDGN
260 270 280 290 300
PNVTPQVTWD VLILQHEHGI NDALEMIDEL RGFLSNSIRY AGATEELLAS
310 320 330 340 350
LQADLERLPE ISPRYKRLNA EEPYRLKATC IRQKLENTKQ RLAKGTPHED
360 370 380 390 400
GRDYLGTAQL IDDLRIVQTS LREHRGGLFA DGRLARTIRT LAAFGLQLAT
410 420 430 440 450
MDVREHADAH HHALGQLFDR LGEESWRYAD MPREYRTKLL AKELRSRRPL
460 470 480 490 500
APSPAPVDAP GEKTLGVFQT VRRALEVFGP EVIESYIISM CQGADDVFAA
510 520 530 540 550
AVLAREAGLI DLHAGWAKIG IVPLLETTDE LKAADTILED LLADPSYRRL
560 570 580 590 600
VALRGDVQEV MLGYSDSSKF GGITTSQWEI HRAQRRLRDV AHRYGVRLRL
610 620 630 640 650
FHGRGGTVGR GGGPTHDAIL AQPWGTLEGE IKVTEQGEVI SDKYLIPALA
660 670 680 690 700
RENLELTVAA TLQASALHTA PRQSDEALAR WDAAMDVVSD AAHTAYRHLV
710 720 730 740 750
EDPDLPTYFL ASTPVDQLAD LHLGSRPSRR PGSGVSLDGL RAIPWVFGWT
760 770 780 790 800
QSRQIVPGWY GVGSGLKALR EAGLDTVLDE MHQQWHFFRN FISNVEMTLA
810 820 830 840 850
KTDLRIAQHY VDTLVPDELK HVFDTIKAEH ELTVAEVLRV TGESELLDAD
860 870 880 890 900
PVLKQTFTIR DAYLDPISYL QVALLGRQRE AAAANEDPDP LLARALLLTV
910
NGVAAGLRNT G
Length:911
Mass (Da):101,297
Last modified:May 1, 2000 - v1
Checksum:i5192E0BB96881273
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF177946 Genomic DNA. Translation: AAD53311.1.
AF160253 Genomic DNA. Translation: AAM54458.1.
AL939115 Genomic DNA. Translation: CAB95920.1.
RefSeqiNP_627344.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB95920; CAB95920; CAB95920.
GeneIDi1098561.
KEGGisco:SCO3127.
PATRICi23736002. VBIStrCoe124346_3191.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF177946 Genomic DNA. Translation: AAD53311.1 .
AF160253 Genomic DNA. Translation: AAM54458.1 .
AL939115 Genomic DNA. Translation: CAB95920.1 .
RefSeqi NP_627344.1. NC_003888.3.

3D structure databases

ProteinModelPortali Q9RNU9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 100226.SCO3127.

Proteomic databases

PRIDEi Q9RNU9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB95920 ; CAB95920 ; CAB95920 .
GeneIDi 1098561.
KEGGi sco:SCO3127.
PATRICi 23736002. VBIStrCoe124346_3191.

Phylogenomic databases

eggNOGi COG2352.
HOGENOMi HOG000238647.
InParanoidi Q9RNU9.
KOi K01595.
OMAi ELSTISC.
OrthoDBi EOG6TJ7T8.
PhylomeDBi Q9RNU9.

Family and domain databases

HAMAPi MF_00595. PEPcase_type1.
InterProi IPR021135. PEP_COase.
IPR018129. PEP_COase_AS.
IPR022805. PEP_COase_bac/pln-type.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view ]
Pfami PF00311. PEPcase. 1 hit.
[Graphical view ]
PRINTSi PR00150. PEPCARBXLASE.
SUPFAMi SSF51621. SSF51621. 1 hit.
PROSITEi PS00781. PEPCASE_1. 1 hit.
PS00393. PEPCASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Phosphoenolpyruvate carboxylase from Streptomyces coelicolor A3(2): purification of the enzyme, cloning of the ppc gene and over-expression of the protein in a streptomycete."
    Bramwell H., Nimmo H.G., Hunter I.S., Coggins J.R.
    Biochem. J. 293:131-136(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: A3(2) / NRRL B-16638.
  2. "The ppc gene of Streptomyces coelicolor A3(2)."
    Ricketts A.D.J., Hunter I.S.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: A3(2) / NRRL B-16638.
  3. "Characterization of the phosphoenolpyruvate carboxylase gene from Streptomyces coelicolor A3(2) and a ppc gene disruption mutant."
    Alves A.M.C.R., te Poele E., White J., Bibb M.J., Dijkhuizen L.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: A3(2) / NRRL B-16638.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.

Entry informationi

Entry nameiCAPP_STRCO
AccessioniPrimary (citable) accession number: Q9RNU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3