Reviewed, UniProtKB/Swiss-Prot Q1QH22 (RBL1A_NITHX)

Names and origin

Protein names

Recommended name:
    Ribulose bisphosphate carboxylase large chain 1
      Short name=RuBisCO large subunit 1
    EC=4.1.1.39

Gene names

Name:	cbbL1
Ordered Locus Names:	Nham_3751

Organism

Nitrobacter hamburgensis (strain X14 / DSM 10229) [Complete proteome] [HAMAP]

Taxonomic identifier

323097 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Nitrobacter

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 By similarity.
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 By similarity.
Subunit structure	Heterohexadecamer of 8 large chains and 8 small chains 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" By similarity.
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
Technical term	Complete proteome
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 – 488	488	Ribulose bisphosphate carboxylase large chain 1 HAMAP MF_01338		PRO_0000251446
Sites
	Active site	180	1	Proton acceptor By similarity
	Active site	298	1	Proton acceptor By similarity
	Metal binding	206	1	Magnesium; via carbamate group By similarity
	Metal binding	208	1	Magnesium By similarity
	Metal binding	209	1	Magnesium By similarity
	Binding site	128	1	Substrate; in homodimeric partner By similarity
	Binding site	178	1	Substrate By similarity
	Binding site	182	1	Substrate By similarity
	Binding site	299	1	Substrate By similarity
	Binding site	331	1	Substrate By similarity
	Binding site	383	1	Substrate By similarity
	Site	338	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	206	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1QH22-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 7E1D8D888F148B44	FASTA	488	54,155
	10 20 30 40 50 60 MNVLNEKSLT VRGKDRYKSG VMSYKKMGYW EPDYTPKDTD IICLFRVTPQ DGVDPIEAAA 70 80 90 100 110 120 AVAGESSTAT WTVVWTDRLT AAEKYRAKCY RVDPVPGAEG QYFAYIAYDL DLFESGSISN 130 140 150 160 170 180 LTASVIGNVF GFKPLKALRL EDMRLPVAYV KTFKGPPTGI VVERERLDKF GRPLLGATVK 190 200 210 220 230 240 PKLGLSGRNY GRVVYEALKG GLDFTKDDEN INSQPFMHWR ERFLYCMEAV NRAQAATGEV 250 260 270 280 290 300 KGSYLNVTAA TMEDMYERAE FAKELGSVVV MIDLVIGYTA IQSMSNWARK NDMILHLHRA 310 320 330 340 350 360 GHSTYTRQRN HGVSFRVISK WMRLAGVDHI HAGTVVGKLE GDPLTTRGYY DICREEHNPM 370 380 390 400 410 420 QLEHGIFFDQ NWASLNKMMP VASGGIHAGQ MHQLIQHLGE DVVLQFGGGT IGHPMGIQAG 430 440 450 460 470 480 AIANRVALEA MILARNEGRD YVSEGPDILA KAAASCTPLK QALEVWKDVT FNYQSTDAPD YVTTPAVA

References

[1]

"Complete sequence of chromosome of Nitrobacter hamburgensis X14." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000319 Genomic DNA. Translation: ABE64475.1.
RefSeq	YP_578935.1.
3D structure databases
SMR	Q1QH22. Positions 16-482.
ModBase	Search...
Genome annotation databases
GeneID	4032488.
GenomeReviews	Gene locus Nham_3751 in contig CP000319_GR.
KEGG	nha:Nham_3751.
NMPDR	fig|323097.3.peg.2227.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1QH22.
Enzyme and pathway databases
BioCyc	NHAM323097:NHAM_3751-MON.
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

RBL1A_NITHX

Accession

Primary (citable) accession number: Q1QH22

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	May 16, 2006
Last modified:	March 24, 2009
This is version 24 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)