RBS_EUGGR
ID RBS_EUGGR Reviewed; 1273 AA.
AC P16881; Q42727;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Ribulose bisphosphate carboxylase small subunit, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00860};
DE Short=RuBisCO small subunit {ECO:0000255|HAMAP-Rule:MF_00860};
DE Contains:
DE RecName: Full=Ribulose bisphosphate carboxylase small chain P1, chloroplastic;
DE Contains:
DE RecName: Full=Ribulose bisphosphate carboxylase small chain P2, chloroplastic;
DE Contains:
DE RecName: Full=Ribulose bisphosphate carboxylase small chain P3, chloroplastic;
DE Contains:
DE RecName: Full=Ribulose bisphosphate carboxylase small chain P4, chloroplastic;
DE Contains:
DE RecName: Full=Ribulose bisphosphate carboxylase small chain P5, chloroplastic;
DE Contains:
DE RecName: Full=Ribulose bisphosphate carboxylase small chain P6, chloroplastic;
DE Contains:
DE RecName: Full=Ribulose bisphosphate carboxylase small chain P7, chloroplastic;
DE Contains:
DE RecName: Full=Ribulose bisphosphate carboxylase small chain P8, chloroplastic;
DE Flags: Precursor;
GN Name=RBCS {ECO:0000255|HAMAP-Rule:MF_00860}; Synonyms=RBCS1;
OS Euglena gracilis.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROBABLE POLYPROTEIN PROCESSING.
RC STRAIN=Z / UTEX 753;
RX PubMed=2105882; DOI=10.1002/j.1460-2075.1990.tb08115.x;
RA Chan R.L., Keller M., Canaday J., Weil J.H., Imbault P.;
RT "Eight small subunits of Euglena ribulose 1-5 bisphosphate
RT carboxylase/oxygenase are translated from a large mRNA as a polyprotein.";
RL EMBO J. 9:333-338(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Z / UTEX 753;
RX PubMed=7823317; DOI=10.1016/s0022-2836(95)80035-2;
RA Tessier L.H., Paulus F., Keller M., Vial C., Imbault P.;
RT "Structure and expression of Euglena gracilis nuclear rbcS genes encoding
RT the small subunits of the ribulose 1,5-bisphosphate carboxylase/oxygenase:
RT a novel splicing process for unusual intervening sequences?";
RL J. Mol. Biol. 245:22-33(1995).
RN [3]
RP PROTEIN SEQUENCE OF 135-138; 266-268; 279-282; 409-411; 422-425; 553-555;
RP 566-569; 696-698; 709-712; 841-843; 854-857; 984-986; 997-1000; 1128-1130
RP AND 1141-1144, AND PROBABLE POLYPROTEIN PROCESSING.
RX PubMed=24302307; DOI=10.1007/bf00021333;
RA Sailland A., Amiri I., Freyssinet G.;
RT "Amino acid sequence of the ribulose-1,5-bisphosphate carboxylase/oxygenase
RT small subunit from Euglena.";
RL Plant Mol. Biol. 7:213-218(1986).
CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC fixation, as well as the oxidative fragmentation of the pentose
CC substrate. Both reactions occur simultaneously and in competition at
CC the same active site. Although the small subunit is not catalytic it is
CC essential for maximal activity. {ECO:0000255|HAMAP-Rule:MF_00860}.
CC -!- SUBUNIT: Heterohexadecamer of 8 large and 8 small subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00860}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_00860, ECO:0000305|PubMed:2105882,
CC ECO:0000305|PubMed:24302307}. Note=In this organism the chloroplast is
CC within a membrane system that is probably derived from the endoplasmic
CC reticulum. The first half of the transit peptide resembles a signal
CC sequence while the second half has the hallmarks of a transit peptide.
CC {ECO:0000305|PubMed:2105882}.
CC -!- PTM: Eight small subunits are processed from a large polyprotein
CC (Probable). All start with the same sequence but there is more
CC heterogeneity at the C-terminus (PubMed:24302307).
CC {ECO:0000269|PubMed:24302307, ECO:0000305|PubMed:2105882,
CC ECO:0000305|PubMed:24302307}.
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC this homodimer is arranged in a barrel-like tetramer with the small
CC subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC {ECO:0000255|HAMAP-Rule:MF_00860}.
CC -!- SIMILARITY: Belongs to the RuBisCO small chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00860}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X17546; CAA35584.1; -; mRNA.
DR EMBL; X79152; CAA55779.1; -; Genomic_DNA.
DR PIR; S53636; S53636.
DR AlphaFoldDB; P16881; -.
DR SMR; P16881; -.
DR SABIO-RK; P16881; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
DR CDD; cd03527; RuBisCO_small; 8.
DR Gene3D; 3.30.190.10; -; 8.
DR HAMAP; MF_00859; RuBisCO_S_bact; 1.
DR InterPro; IPR024681; RuBisCO_ssu.
DR InterPro; IPR000894; RuBisCO_ssu_dom.
DR InterPro; IPR036385; RuBisCO_ssu_sf.
DR PANTHER; PTHR31262; PTHR31262; 8.
DR Pfam; PF00101; RuBisCO_small; 8.
DR PRINTS; PR00152; RUBISCOSMALL.
DR SMART; SM00961; RuBisCO_small; 8.
DR SUPFAM; SSF55239; SSF55239; 8.
PE 1: Evidence at protein level;
KW Calvin cycle; Carbon dioxide fixation; Chloroplast;
KW Direct protein sequencing; Photorespiration; Photosynthesis; Plastid;
KW Repeat; Transit peptide.
FT TRANSIT 1..134
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:24302307"
FT CHAIN 135..268
FT /note="Ribulose bisphosphate carboxylase small chain P1,
FT chloroplastic"
FT /id="PRO_0000031476"
FT PROPEP 269..278
FT /id="PRO_0000031477"
FT CHAIN 279..411
FT /note="Ribulose bisphosphate carboxylase small chain P2,
FT chloroplastic"
FT /id="PRO_0000031478"
FT PROPEP 412..421
FT /id="PRO_0000031479"
FT CHAIN 422..555
FT /note="Ribulose bisphosphate carboxylase small chain P3,
FT chloroplastic"
FT /id="PRO_0000031480"
FT PROPEP 556..565
FT /id="PRO_0000031481"
FT CHAIN 566..698
FT /note="Ribulose bisphosphate carboxylase small chain P4,
FT chloroplastic"
FT /id="PRO_0000031482"
FT PROPEP 699..708
FT /id="PRO_0000031483"
FT CHAIN 709..843
FT /note="Ribulose bisphosphate carboxylase small chain P5,
FT chloroplastic"
FT /id="PRO_0000031484"
FT PROPEP 844..853
FT /id="PRO_0000031485"
FT CHAIN 854..986
FT /note="Ribulose bisphosphate carboxylase small chain P6,
FT chloroplastic"
FT /id="PRO_0000031486"
FT PROPEP 987..996
FT /id="PRO_0000031487"
FT CHAIN 997..1130
FT /note="Ribulose bisphosphate carboxylase small chain P7,
FT chloroplastic"
FT /id="PRO_0000031488"
FT PROPEP 1131..1140
FT /id="PRO_0000031489"
FT CHAIN 1141..1273
FT /note="Ribulose bisphosphate carboxylase small chain P8,
FT chloroplastic"
FT /id="PRO_0000031490"
FT CONFLICT 410
FT /note="S -> SS (in Ref. 2; CAA55779)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="H -> R (in Ref. 2; CAA55779)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="D -> E (in Ref. 2; CAA55779)"
FT /evidence="ECO:0000305"
FT CONFLICT 697
FT /note="S -> SS (in Ref. 2; CAA55779)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="Missing (in Ref. 2; CAA55779)"
FT /evidence="ECO:0000305"
FT CONFLICT 961
FT /note="A -> AA (in Ref. 2; CAA55779)"
FT /evidence="ECO:0000305"
FT CONFLICT 996
FT /note="D -> E (in Ref. 2; CAA55779)"
FT /evidence="ECO:0000305"
FT CONFLICT 1140
FT /note="E -> D (in Ref. 2; CAA55779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1273 AA; 141868 MW; EC0CA149519F6E04 CRC64;
MPFDRQPLLS GEKGMPATSL WLVGGAVIAA VCVIVNTSYN GTQLSVTARP IQAAVSQVSM
ARFAESGVSR GSGNRVSQAV PLMAASVGAE SESRRWVASA ILFPLSGLFA AVALKMAMMK
PKVAAVLPFT SEKDMKVWNP VNNKKFETFS YLPPLSDAQI AKQVDMIIAK GLSPCLEFAA
PENSFIANDN TVRFSGTAAG YYDNRYWTMW KLPMFGCTDA SQVLREISEC RRAYPQCYVR
LAAFDSVKQV QVISFVVQRP SGSSSSSWGM AAMTGEKDMK VWNPVNNKKF ETFSYLPPLS
DAQIAKQVDM IIAKGLSPCL EFAAPENSFI ANDNTVRFSG TAAGYYDNRY WTMWKLPMFG
CTDASQVLRE ISECRRAYPQ CYVRLAAFDS VKQVQVISFV VQRPSGSSSS WGMAAMTGEK
DMKVWNPVNN KKFETFSYLP PLSDAQIAKQ VDMIIAKGLS PCLEFAAPEN SFIANDNTVR
FSGTAAGYYD NHYWTMWKLP MFGCTDASQV LREISECRRA YPQCYVRLAA FDSVKQVQVI
SFVVQRPSGS SSSSWGMAAM TGEKDMKVWN PVNNKKFETF SYLPPLSDAQ IAKQVDMIIA
KGLSPCLEFA APENSFIAND NTVRFSGTAA GYYDNRYWTM WKLPMFGCTD ASQVLREISE
CRRAYPQCYV RLAAFDSVKQ VQVISFVVQR PSGSSSSWGM AAMTGEKDMK VWNPVNNKKF
ETFSYLPPLS DAQIAKQVDM IIAKGLSPCL EFAAPENSFI ANDNTVRFSG TAAGYYDNRY
WTMWKLPMFG CTDASQVLRE ISECRRAYPQ CYVRLAAFDS VKQVQVISFV VQRPSGSSSS
SSWGMAAMTG EKEMKVWNPV NNKKFETFSY LPPLSDAQIA KQVDMIIAKG LSPCLEFAAP
ENSFIANDNT VRFSGTAAGY YDNRYWTMWK LPMFGCTDAS QVLREISECR RAYPQCYVRL
AFDSVKQVQV ISFVVQRPSG SSSSSWGMAA MTGEKDMKVW NPVNNKKFET FSYLPPLSDA
QIAKQVDMII AKGLSPCLEF AAPENSFIAN DNTVRFSGTA AGYYDNRYWT MWKLPMFGCT
DASQVLREIS ECRRAYPQCY VRLAAFDSVK QVQVISFVVQ RPSGSSSSSW GMAAMTGEKE
MKVWNPVNNK KFETFSYLPP LSDAQIAKQV DMIIAKGLSP CLEFAAPENS FIANDNTVRF
SGTAAGYYDN RYWTMWKLPM FGCTDASQVL REISECRRAY PQCYVRLAAF DSVKQVQVIS
FVVQRPSSGG RSW
