NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MS-1;
DOI=10.1007/s00203-004-0716-y; PubMed=15338111 [NCBI, ExPASy, EBI, Israel, Japan]
Bazylinski D.A., Dean A.J., Williams T.J., Long L.K., Middleton S.L., Dubbels B.L.;
"Chemolithoautotrophy in the marine, magnetotactic bacterial strains MV-1 and MV-2.";
Arch. Microbiol. 182:373-387(2004).

Comments

FUNCTION: 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).
CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H⁺ = D-ribulose 1,5-bisphosphate + CO₂ + H₂O.
CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O₂.
COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
MISCELLANEOUS: The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits (By similarity).
SIMILARITY: Belongs to the RuBisCO large chain family. Type II subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF442517; AAL76920.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P04718; 1RBA. [HSSP ENTRY / PDB]

SMR

Q8RTI2; 2-457.

ModBase

Q8RTI2.

Ontologies

GO:0009573;	Cellular component: chloroplast ribulose bisphosphate carboxylase complex (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004497;	Molecular function: monooxygenase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0016984;	Molecular function: ribulose-bisphosphate carboxylase activity (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019253;	Biological process: reductive pentose-phosphate cycle (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01339; -; 1.
PBIL [Tree]

InterPro

IPR000685; RuBisCO_lsu_C.
IPR017443; RuBisCO_lsu_fd_N.
IPR017444; RuBisCO_lsu_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.110; RuBisCO_large; 1.
G3DSA:3.30.70.150; RuBisCO_large; 1.

Pfam

PF00016; RuBisCO_large; 1.
PF02788; RuBisCO_large_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00157; RUBISCO_LARGE; 1.

ProtoNet

Q8RTI2.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calvin cycle; Carbon dioxide fixation; Lyase; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 459`	`459`	`Ribulose bisphosphate carboxylase.`	`PRO_0000062663`
`ACT_SITE`	`166 166`		`Proton acceptor (By similarity).`
`ACT_SITE`	`287 287`		`Proton acceptor (By similarity).`
`METAL`	`191 191`		`Magnesium; via carbamate group (By similarity).`
`METAL`	`193 193`		`Magnesium (By similarity).`
`METAL`	`194 194`		`Magnesium (By similarity).`
`BINDING`	`111 111`		`Substrate; in homodimeric partner (By similarity).`
`BINDING`	`168 168`		`Substrate (By similarity).`
`BINDING`	`288 288`		`Substrate (By similarity).`
`BINDING`	`321 321`		`Substrate (By similarity).`
`BINDING`	`368 368`		`Substrate (By similarity).`
`SITE`	`329 329`	`1`	`Transition state stabilizer (By similarity).`
`MOD_RES`	`191 191`		`N6-carboxylysine (By similarity).`

Sequence information

Length: 459 AA [This is the length of the unprocessed precursor]

Molecular weight: 50217 Da [This is the MW of the unprocessed precursor]

CRC64: 7BAF901EE932774F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDQSKRYVNL ALSEADLIKG GRHVLCAYRM RPRPGHGYVE TAAHFAAESS TGTNVEVCTT 

        70         80         90        100        110        120 
DDFTRGVDAL VYEVDEAEGL MKIAYPVDLF DRNIIDGKAM IASFLTLTVG NNQGMSDVEN 

       130        140        150        160        170        180 
AKMEDFYVPP EFLKLFDGPA CNISHMWKVL GRPEVNGGMV VGTIIKPKLG LRPKPFADAC 

       190        200        210        220        230        240 
HQFWLGGDFI KNDEPQGNQV FAPLKETMRL VADAMRRAQD ETGVPKLLSA NITADDPAEM 

       250        260        270        280        290        300 
IARGNFILET FGENASHVAF LVDGFVAGPT AVTTCRRNFP DTFLHYHRAG HGAITSRQSK 

       310        320        330        340        350        360 
RGYTVLVHMK MARLLGASGI HTGTMGYGKM EGAPDEKMVA YMLERQIAEG PYYRQDWGGM 

       370        380        390        400        410        420 
ASCTPIISGG MSALRLPGFF DNLGHSNVIQ TSGGGAFGHK DGAIAGALSL RQAHEAWLKK 

       430        440        450 
IDLVDYAQTH AELRGAFESF ASDADRLYPG WRDRLRIAA

Q8RTI2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools