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Protein

Ribulose bisphosphate carboxylase small chains, chloroplastic

Gene

RBCS1

Organism
Euglena gracilis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site (By similarity).By similarity

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Enzyme and pathway databases

SABIO-RKP16881.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:RBCS1
Synonyms:RBCS
OrganismiEuglena gracilis
Taxonomic identifieri3039 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaEuglenidaEuglenalesEuglenaceaeEuglena

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 134134ChloroplastAdd
BLAST
Chaini135 – 268134Ribulose bisphosphate carboxylase small chain P1, chloroplasticPRO_0000031476Add
BLAST
Propeptidei269 – 27810PRO_0000031477
Chaini279 – 411133Ribulose bisphosphate carboxylase small chain P2, chloroplasticPRO_0000031478Add
BLAST
Propeptidei412 – 42110PRO_0000031479
Chaini422 – 555134Ribulose bisphosphate carboxylase small chain P3, chloroplasticPRO_0000031480Add
BLAST
Propeptidei556 – 56510PRO_0000031481
Chaini566 – 698133Ribulose bisphosphate carboxylase small chain P4, chloroplasticPRO_0000031482Add
BLAST
Propeptidei699 – 70810PRO_0000031483
Chaini709 – 843135Ribulose bisphosphate carboxylase small chain P5, chloroplasticPRO_0000031484Add
BLAST
Propeptidei844 – 85310PRO_0000031485
Chaini854 – 986133Ribulose bisphosphate carboxylase small chain P6, chloroplasticPRO_0000031486Add
BLAST
Propeptidei987 – 99610PRO_0000031487
Chaini997 – 1130134Ribulose bisphosphate carboxylase small chain P7, chloroplasticPRO_0000031488Add
BLAST
Propeptidei1131 – 114010PRO_0000031489
Chaini1141 – 1273133Ribulose bisphosphate carboxylase small chain P8, chloroplasticPRO_0000031490Add
BLAST

Post-translational modificationi

Eight small subunits are processed from a large polyprotein.

Interactioni

Subunit structurei

8 large chains + 8 small chains.

Structurei

3D structure databases

ProteinModelPortaliP16881.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO small chain family.Curated

Keywords - Domaini

Repeat, Transit peptide

Family and domain databases

Gene3Di3.30.190.10. 8 hits.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamiPF00101. RuBisCO_small. 8 hits.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SMARTiSM00961. RuBisCO_small. 8 hits.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 8 hits.

Sequencei

Sequence statusi: Complete.

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

P16881-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFDRQPLLS GEKGMPATSL WLVGGAVIAA VCVIVNTSYN GTQLSVTARP
60 70 80 90 100
IQAAVSQVSM ARFAESGVSR GSGNRVSQAV PLMAASVGAE SESRRWVASA
110 120 130 140 150
ILFPLSGLFA AVALKMAMMK PKVAAVLPFT SEKDMKVWNP VNNKKFETFS
160 170 180 190 200
YLPPLSDAQI AKQVDMIIAK GLSPCLEFAA PENSFIANDN TVRFSGTAAG
210 220 230 240 250
YYDNRYWTMW KLPMFGCTDA SQVLREISEC RRAYPQCYVR LAAFDSVKQV
260 270 280 290 300
QVISFVVQRP SGSSSSSWGM AAMTGEKDMK VWNPVNNKKF ETFSYLPPLS
310 320 330 340 350
DAQIAKQVDM IIAKGLSPCL EFAAPENSFI ANDNTVRFSG TAAGYYDNRY
360 370 380 390 400
WTMWKLPMFG CTDASQVLRE ISECRRAYPQ CYVRLAAFDS VKQVQVISFV
410 420 430 440 450
VQRPSGSSSS WGMAAMTGEK DMKVWNPVNN KKFETFSYLP PLSDAQIAKQ
460 470 480 490 500
VDMIIAKGLS PCLEFAAPEN SFIANDNTVR FSGTAAGYYD NHYWTMWKLP
510 520 530 540 550
MFGCTDASQV LREISECRRA YPQCYVRLAA FDSVKQVQVI SFVVQRPSGS
560 570 580 590 600
SSSSWGMAAM TGEKDMKVWN PVNNKKFETF SYLPPLSDAQ IAKQVDMIIA
610 620 630 640 650
KGLSPCLEFA APENSFIAND NTVRFSGTAA GYYDNRYWTM WKLPMFGCTD
660 670 680 690 700
ASQVLREISE CRRAYPQCYV RLAAFDSVKQ VQVISFVVQR PSGSSSSWGM
710 720 730 740 750
AAMTGEKDMK VWNPVNNKKF ETFSYLPPLS DAQIAKQVDM IIAKGLSPCL
760 770 780 790 800
EFAAPENSFI ANDNTVRFSG TAAGYYDNRY WTMWKLPMFG CTDASQVLRE
810 820 830 840 850
ISECRRAYPQ CYVRLAAFDS VKQVQVISFV VQRPSGSSSS SSWGMAAMTG
860 870 880 890 900
EKEMKVWNPV NNKKFETFSY LPPLSDAQIA KQVDMIIAKG LSPCLEFAAP
910 920 930 940 950
ENSFIANDNT VRFSGTAAGY YDNRYWTMWK LPMFGCTDAS QVLREISECR
960 970 980 990 1000
RAYPQCYVRL AFDSVKQVQV ISFVVQRPSG SSSSSWGMAA MTGEKDMKVW
1010 1020 1030 1040 1050
NPVNNKKFET FSYLPPLSDA QIAKQVDMII AKGLSPCLEF AAPENSFIAN
1060 1070 1080 1090 1100
DNTVRFSGTA AGYYDNRYWT MWKLPMFGCT DASQVLREIS ECRRAYPQCY
1110 1120 1130 1140 1150
VRLAAFDSVK QVQVISFVVQ RPSGSSSSSW GMAAMTGEKE MKVWNPVNNK
1160 1170 1180 1190 1200
KFETFSYLPP LSDAQIAKQV DMIIAKGLSP CLEFAAPENS FIANDNTVRF
1210 1220 1230 1240 1250
SGTAAGYYDN RYWTMWKLPM FGCTDASQVL REISECRRAY PQCYVRLAAF
1260 1270
DSVKQVQVIS FVVQRPSSGG RSW
Length:1,273
Mass (Da):141,868
Last modified:August 1, 1990 - v1
Checksum:iEC0CA149519F6E04
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti410 – 4101S → SS in CAA55779 (PubMed:7823317).Curated
Sequence conflicti492 – 4921H → R in CAA55779 (PubMed:7823317).Curated
Sequence conflicti565 – 5651D → E in CAA55779 (PubMed:7823317).Curated
Sequence conflicti697 – 6971S → SS in CAA55779 (PubMed:7823317).Curated
Sequence conflicti842 – 8421Missing in CAA55779 (PubMed:7823317).Curated
Sequence conflicti961 – 9611A → AA in CAA55779 (PubMed:7823317).Curated
Sequence conflicti996 – 9961D → E in CAA55779 (PubMed:7823317).Curated
Sequence conflicti1140 – 11401E → D in CAA55779 (PubMed:7823317).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17546 mRNA. Translation: CAA35584.1.
X79152 Genomic DNA. Translation: CAA55779.1.
PIRiS53636.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17546 mRNA. Translation: CAA35584.1.
X79152 Genomic DNA. Translation: CAA55779.1.
PIRiS53636.

3D structure databases

ProteinModelPortaliP16881.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP16881.

Family and domain databases

Gene3Di3.30.190.10. 8 hits.
InterProiIPR024681. RuBisCO_sc.
IPR000894. RuBisCO_sc_dom.
[Graphical view]
PfamiPF00101. RuBisCO_small. 8 hits.
[Graphical view]
PRINTSiPR00152. RUBISCOSMALL.
SMARTiSM00961. RuBisCO_small. 8 hits.
[Graphical view]
SUPFAMiSSF55239. SSF55239. 8 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiRBS_EUGGR
AccessioniPrimary (citable) accession number: P16881
Secondary accession number(s): Q42727
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 13, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. 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.