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Q0AHW1

- RBL_NITEC

UniProt

Q0AHW1 - RBL_NITEC

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Nitrosomonas eutropha (strain C91)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg(2+) ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161Substrate; in homodimeric partnerUniRule annotation
Binding sitei166 – 1661SubstrateUniRule annotation
Active sitei168 – 1681Proton acceptorUniRule annotation
Binding sitei170 – 1701SubstrateUniRule annotation
Metal bindingi194 – 1941Magnesium; via carbamate groupUniRule annotation
Metal bindingi196 – 1961MagnesiumUniRule annotation
Metal bindingi197 – 1971MagnesiumUniRule annotation
Active sitei287 – 2871Proton acceptorUniRule annotation
Binding sitei288 – 2881SubstrateUniRule annotation
Binding sitei320 – 3201SubstrateUniRule annotation
Sitei327 – 3271Transition state stabilizerUniRule annotation
Binding sitei372 – 3721SubstrateUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciNEUT335283:GHT6-821-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:cbbLUniRule annotation
Ordered Locus Names:Neut_0804
OrganismiNitrosomonas eutropha (strain C91)
Taxonomic identifieri335283 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
ProteomesiUP000001966: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Ribulose bisphosphate carboxylase large chainPRO_0000299966Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941N6-carboxylysineUniRule annotation

Proteomic databases

PRIDEiQ0AHW1.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

Protein-protein interaction databases

STRINGi335283.Neut_0804.

Structurei

3D structure databases

ProteinModelPortaliQ0AHW1.
SMRiQ0AHW1. Positions 16-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiMETWKEV.
OrthoDBiEOG6ZKXMS.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.

Sequencei

Sequence statusi: Complete.

Q0AHW1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAIKTYQAGV KEYRQTYWQP DYVPLDTDIL ACFKITPQSG VDREEAAAAV
60 70 80 90 100
AAESSCGTWT TVWTDLLTDL DYYKGRAYRI EDVPGDDARF YAFVAYPIDL
110 120 130 140 150
FEEGSVVNVF TSLVGNVFGF KAIRALRLED VRFPIAYVKT CGGPPSGIQV
160 170 180 190 200
ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGSL DFTKDDENIN
210 220 230 240 250
SQPFMRWRDR FEFVQEATLK AEAETGERKG HYLNVTAPTP EEMYKRAEFA
260 270 280 290 300
KEIGAPIIMH DYLAGGLCAN AGLANWCRNN GMLLHVHRAM HAVLDRNPHH
310 320 330 340 350
GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESFVPED
360 370 380 390 400
RSRGIFFDQD WGSMPGAFAV ASGGIHVWHM PALVAIFGDD SVLQFGGGTL
410 420 430 440 450
GHPWGNAAGA HANRVALEAC VQARNEGRQI EKEGREILTA AAQHSPELKI
460 470
AMETWKEIKF EFDTVDKLDI AHK
Length:473
Mass (Da):52,688
Last modified:October 17, 2006 - v1
Checksum:i0E1D9FEAF68426BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000450 Genomic DNA. Translation: ABI59071.1.
RefSeqiYP_747036.1. NC_008344.1.

Genome annotation databases

EnsemblBacteriaiABI59071; ABI59071; Neut_0804.
GeneIDi4272958.
KEGGinet:Neut_0804.
PATRICi22718721. VBINitEut7577_1030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000450 Genomic DNA. Translation: ABI59071.1 .
RefSeqi YP_747036.1. NC_008344.1.

3D structure databases

ProteinModelPortali Q0AHW1.
SMRi Q0AHW1. Positions 16-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 335283.Neut_0804.

Proteomic databases

PRIDEi Q0AHW1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABI59071 ; ABI59071 ; Neut_0804 .
GeneIDi 4272958.
KEGGi net:Neut_0804.
PATRICi 22718721. VBINitEut7577_1030.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi METWKEV.
OrthoDBi EOG6ZKXMS.

Enzyme and pathway databases

BioCyci NEUT335283:GHT6-821-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas eutropha C91: implications for niche adaptation."
    Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.
    Environ. Microbiol. 9:2993-3007(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C91.

Entry informationi

Entry nameiRBL_NITEC
AccessioniPrimary (citable) accession number: Q0AHW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 17, 2006
Last modified: November 26, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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".UniRule annotation

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3