Reviewed, UniProtKB/Swiss-Prot P04718 (RBL2_RHORU)

Names and origin

Protein names

Recommended name:
    Ribulose bisphosphate carboxylase
      Short name=RuBisCO
    EC=4.1.1.39

Gene names

Name:	cbbM
Synonyms:	cbbL2, rbpL

Organism

Rhodospirillum rubrum

Taxonomic identifier

1085 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Rhodospirillum

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (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. HAMAP MF_01339
Catalytic activity	2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP MF_01339 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP MF_01339
Cofactor	Binds 1 magnesium ion per subunit. Ref.6
Subunit structure	Homodimer. Ref.6
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. HAMAP MF_01339
Sequence similarities	Belongs to the RuBisCO large chain family. Type II subfamily.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation Photosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plastid Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 466

466

Ribulose bisphosphate carboxylase HAMAP MF_01339

PRO_0000062666

Sites

Active site

166

1

Proton acceptor HAMAP MF_01339

Active site

287

1

Proton acceptor HAMAP MF_01339

Metal binding

191

1

Magnesium; via carbamate group HAMAP MF_01339

Metal binding

193

1

Magnesium HAMAP MF_01339

Metal binding

194

1

Magnesium HAMAP MF_01339

Binding site

111

1

Substrate; in homodimeric partner HAMAP MF_01339

Binding site

168

1

Substrate HAMAP MF_01339

Binding site

288

1

Substrate HAMAP MF_01339

Binding site

321

1

Substrate HAMAP MF_01339

Binding site

368

1

Substrate HAMAP MF_01339

Site

329

1

Transition state stabilizer HAMAP MF_01339

Amino acid modifications

Modified residue

191

1

N6-carboxylysine HAMAP MF_01339

Secondary structure

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466

Helix Strand Turn

Details...

Turn

4 – 6

3

Helix

14 – 19

6

Beta strand

23 – 32

10

Beta strand

34 – 36

3

Helix

38 – 48

11

Turn

49 – 51

3

Beta strand

70 – 75

6

Turn

76 – 79

4

Beta strand

80 – 86

7

Helix

87 – 89

3

Turn

94 – 96

3

Helix

101 – 108

8

Beta strand

118 – 127

10

Helix

130 – 133

4

Helix

143 – 150

8

Beta strand

154 – 156

3

Beta strand

160 – 164

5

Beta strand

166 – 169

4

Helix

173 – 184

12

Beta strand

188 – 191

4

Helix

204 – 222

19

Beta strand

227 – 231

5

Helix

237 – 251

15

Helix

252 – 257

6

Beta strand

258 – 262

5

Turn

264 – 267

4

Helix

269 – 278

10

Beta strand

284 – 286

3

Helix

291 – 293

3

Beta strand

301 – 303

3

Helix

305 – 315

11

Beta strand

318 – 323

6

Helix

337 – 344

8

Beta strand

346 – 349

4

Beta strand

354 – 356

3

Beta strand

364 – 369

6

Turn

373 – 375

3

Helix

376 – 383

8

Beta strand

388 – 392

5

Turn

394 – 397

4

Helix

403 – 419

17

Helix

423 – 428

6

Helix

431 – 439

9

Helix

441 – 447

7

Helix

449 – 451

3

Helix

452 – 455

4

Sequences

	Sequence		Length	Mass (Da)
	P04718-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 37D8C0076CAF7D54	FASTA	466	50,504
	10 20 30 40 50 60 MDQSSRYVNL ALKEEDLIAG GEHVLCAYIM KPKAGYGYVA TAAHFAAESS TGTNVEVCTT 70 80 90 100 110 120 DDFTRGVDAL VYEVDEAREL TKIAYPVALF HRNITDGKAM IASFLTLTMG NNQGMGDVEY 130 140 150 160 170 180 AKMHDFYVPE AYRALFDGPS VNISALWKVL GRPEVDGGLV VGTIIKPKLG LRPKPFAEAC 190 200 210 220 230 240 HAFWLGGDFI KNDEPQGNQP FAPLRDTIAL VADAMRRAQD ETGEAKLFSA NITADDPFEI 250 260 270 280 290 300 IARGEYVLET FGENASHVAL LVDGYVAGAA AITTARRRFP DNFLHYHRAG HGAVTSPQSK 310 320 330 340 350 360 RGYTAFVHCK MARLQGASGI HTGTMGFGKM EGESSDRAIA YMLTQDEAQG PFYRQSWGGM 370 380 390 400 410 420 KACTPIISGG MNALRMPGFF ENLGNANVIL TAGGGAFGHI DGPVAGARSL RQAWQAWRDG 430 440 450 460 VPVLDYAREH KELARAFESF PGDADQIYPG WRKALGVEDT RSALPA

References

[1]	"Nucleotide sequence of the ribulosebisphosphate carboxylase gene from Rhodospirillum rubrum." Nargang F., McIntosh L., Somerville C.R. Mol. Gen. Genet. 193:220-224(1984) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Isolation and sequencing of an active-site peptide from Rhodospirillum rubrum ribulosebisphosphate carboxylase/oxygenase after affinity labeling with 2-[(bromoacetyl)amino]pentitol 1,5-bisphosphate." Fraij B., Hartman F.C. Biochemistry 22:1515-1520(1983) [PubMed: 6404301] [Abstract] Cited for: PROTEIN SEQUENCE OF 314-337.
[3]	"Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9-A resolution." Schneider G., Lindqvist Y., Braenden C.-I., Lorimer G. EMBO J. 5:3409-3415(1986) [PubMed: 16453738] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[4]	"Crystal structure of the active site of ribulose-bisphosphate carboxylase." Andersson I., Knight S., Schneider G., Lindqvist Y., Lundqvist T., Braenden C.-I., Lorimer G.H. Nature 337:229-234(1989) Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[5]	"Crystallographic refinement and structure of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum at 1.7-A resolution." Schneider G., Lindqvist Y., Lundqvist T. J. Mol. Biol. 211:989-1008(1990) [PubMed: 2107319] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[6]	"Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution." Lundqvist T., Schneider G. Biochemistry 30:904-908(1991) [PubMed: 1899197] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), COFACTOR, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X00286 Genomic DNA. Translation: CAA25080.1.

PIR

S07295.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RBA	X-ray	2.60	A/B	1-466	[»]
1RUS	X-ray	2.90	A/B	1-466	[»]
2RUS	X-ray	2.30	A/B	1-466	[»]
5RUB	X-ray	1.70	A/B	1-466	[»]
9RUB	X-ray	2.60	A/B	1-466	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13280.

BRENDA

4.1.1.39. 1671.

Family and domain databases

HAMAP

MF_01339. RuBisCO_L_type2.
[Tree]

InterPro

IPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]

Gene3D

G3DSA:3.20.20.110. RuBisCO_large. 1 hit.
G3DSA:3.30.70.150. RuBisCO_large. 1 hit.

Pfam

PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]

PROSITE

PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RBL2_RHORU

Accession

Primary (citable) accession number: P04718
Secondary accession number(s): P19365, P72313

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	January 19, 2010
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)