Reviewed, UniProtKB/Swiss-Prot P0C2C2 (RBL1C_RALEU)

Names and origin

Protein names

Recommended name:
    Ribulose bisphosphate carboxylase large chain, chromosomal
      Short name=RuBisCO large subunit
    EC=4.1.1.39

Gene names

Name:	cbbL1
Synonyms:	cbbL, cbxLC, cfxLC

Organism

Ralstonia eutropha (Alcaligenes eutrophus)

Taxonomic identifier

106590 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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_01338
Catalytic activity	2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP MF_01338 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP MF_01338
Cofactor	Binds 1 magnesium ion per subunit. HAMAP MF_01338
Subunit structure	Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers. HAMAP MF_01338
Post-translational modification	The disulfide bond which can form between Cys-278 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover By similarity.
Miscellaneous	The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel". HAMAP MF_01338
Sequence similarities	Belongs to the RuBisCO large chain family. Type I subfamily.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure
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
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 – 486

486

Ribulose bisphosphate carboxylase large chain, chromosomal HAMAP MF_01338

PRO_0000062641

Sites

Active site

178

1

Proton acceptor HAMAP MF_01338

Active site

296

1

Proton acceptor HAMAP MF_01338

Metal binding

204

1

Magnesium; via carbamate group HAMAP MF_01338

Metal binding

206

1

Magnesium HAMAP MF_01338

Metal binding

207

1

Magnesium HAMAP MF_01338

Binding site

126

1

Substrate; in homodimeric partner HAMAP MF_01338

Binding site

176

1

Substrate HAMAP MF_01338

Binding site

180

1

Substrate HAMAP MF_01338

Binding site

297

1

Substrate HAMAP MF_01338

Binding site

329

1

Substrate HAMAP MF_01338

Binding site

381

1

Substrate HAMAP MF_01338

Site

336

1

Transition state stabilizer HAMAP MF_01338

Amino acid modifications

Modified residue

204

1

N6-carboxylysine HAMAP MF_01338

Secondary structure

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486

Helix Strand Turn

Details...

Turn

25 – 27

3

Beta strand

38 – 47

10

Helix

53 – 62

10

Turn

63 – 66

4

Helix

75 – 78

4

Helix

81 – 83

3

Beta strand

86 – 92

7

Beta strand

100 – 107

8

Helix

108 – 110

3

Helix

116 – 124

9

Helix

127 – 129

3

Beta strand

133 – 135

3

Beta strand

137 – 142

6

Helix

145 – 148

4

Helix

158 – 165

8

Beta strand

172 – 176

5

Helix

185 – 197

13

Beta strand

201 – 204

4

Helix

217 – 235

19

Beta strand

240 – 244

5

Helix

250 – 262

13

Beta strand

266 – 271

6

Helix

272 – 274

3

Helix

276 – 287

12

Turn

288 – 290

3

Beta strand

292 – 296

5

Turn

298 – 300

3

Helix

301 – 304

4

Beta strand

309 – 311

3

Helix

313 – 323

11

Beta strand

326 – 329

4

Beta strand

335 – 338

4

Helix

341 – 352

12

Beta strand

354 – 356

3

Helix

360 – 362

3

Beta strand

377 – 383

7

Helix

386 – 388

3

Helix

389 – 396

8

Beta strand

401 – 404

4

Helix

406 – 409

4

Helix

414 – 435

22

Helix

439 – 453

15

Helix

455 – 463

9

Sequences

	Sequence		Length	Mass (Da)
	P0C2C2-1 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 66EAB4A11982FAB5	FASTA	486	53,840
	10 20 30 40 50 60 MNAPETIQAK PRKRYDAGVM KYKEMGYWDG DYVPKDTDVL ALFRITPQDG VDPVEAAAAV 70 80 90 100 110 120 AGESSTATWT VVWTDRLTAC DMYRAKAYRV DPVPNNPEQF FCYVAYDLSL FEEGSIANLT 130 140 150 160 170 180 ASIIGNVFSF KPIKAARLED MRFPVAYVKT FAGPSTGIIV ERERLDKFGR PLLGATTKPK 190 200 210 220 230 240 LGLSGRNYGR VVYEGLKGGL DFMKDDENIN SQPFMHWRDR FLFVMDAVNK ASAATGEVKG 250 260 270 280 290 300 SYLNVTAGTM EEMYRRAEFA KSLGSVIIMV DLIVGWTCIQ SMSNWCRQND MILHLHRAGH 310 320 330 340 350 360 GTYTRQKNHG VSFRVIAKWL RLAGVDHMHT GTAVGKLEGD PLTVQGYYNV CRDAYTQTDL 370 380 390 400 410 420 TRGLFFDQDW ASLRKVMPVA SGGIHAGQMH QLIHLFGDDV VLQFGGGTIG HPQGIQAGAT 430 440 450 460 470 480 ANRVALEAMV LARNEGRDIL NEGPEILRDA ARWCAPLRAA LDTWGDITFN YTPTDTSDFV PTASVA

References

[1]	"Sequence analysis of the Alcaligenes eutrophus chromosomally encoded ribulose bisphosphate carboxylase large and small subunit genes and their gene products." Andersen K., Caton J. J. Bacteriol. 169:4547-4558(1987) [PubMed: 2820933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R.
[2]	Andersen K. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"The crystal structure of rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded beta-barrel formed by beta-strands from four subunits." Hansen S., Vollan V.B., Hough E., Andersen K. J. Mol. Biol. 288:609-621(1999) [PubMed: 10329167] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). Strain: ATCC 17707 / LMG 1207 / Stanier 345 / H-20-R.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M17744 Genomic DNA. Translation: AAC28129.1.

PIR

RKALLE. A26954.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BXN	X-ray	2.70	A/C/E/G	1-486	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

4.1.1.39. 1263.

Family and domain databases

HAMAP

MF_01338.
[Tree]

InterPro

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

RBL1C_RALEU

Accession

Primary (citable) accession number: P0C2C2
Secondary accession number(s): P09657, P77811

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	January 23, 2007
Last modified:	March 24, 2009
This is version 21 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)