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Q72S00 (NRDJ_LEPIC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vitamin B12-dependent ribonucleotide reductase

EC=1.17.4.1
Alternative name(s):
Ribonucleoside-diphosphate reductase NrdJ
Gene names
Name:nrdJ
Ordered Locus Names:LIC_11587
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) [Complete proteome] [HAMAP]
Taxonomic identifier267671 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length1201 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen By similarity.

Catalytic activity

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Cofactor

5'-deoxyadenosylcobalamine (coenzyme B12) By similarity.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase class-2 family.

Sequence caution

The sequence AAS70183.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12011201Vitamin B12-dependent ribonucleotide reductase
PRO_0000231659

Regions

Region198 – 1992Substrate binding By similarity
Region482 – 4865Substrate binding By similarity
Region683 – 6875Substrate binding By similarity

Sites

Active site4821Proton acceptor By similarity
Active site4841Cysteine radical intermediate By similarity
Active site4861Proton acceptor By similarity
Binding site1531Substrate By similarity
Binding site2301Substrate; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond199 ↔ 495Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q72S00 [UniParc].

Last modified August 10, 2010. Version 2.
Checksum: 062F88B39A9A120C

FASTA1,201133,918
        10         20         30         40         50         60 
MKMNRHFTVP QNGESSTIQW TKRNSKITNP DGSKVFEAND ILVPEDWSQV AVDILAQKYF 

        70         80         90        100        110        120 
RRKGVPKYLK KVQEDGIPEW LQKSIPDTEK LESLKPEDRF GGETSALEVF HRLAGCWTYW 

       130        140        150        160        170        180 
GYKYKYFSDE ESAKIFYDEI VYMLATQMAA PNSPQWFNTG LNWAYGIDGK SQGHYYVDPS 

       190        200        210        220        230        240 
TGKLVKSTSA YEHPQPHACF IQSVDDDLVN EGGIMDLWVR EARLFKYGSG TGTNFSNLRG 

       250        260        270        280        290        300 
ENEPLSGGGK SSGLMSFLKI GDRAAGAIKS GGTTRRAAKM VCLDVDHPDI ENFIDWKVTE 

       310        320        330        340        350        360 
EKKVASLVTG SMLNNRHLNA IMSACYEMEG EDRFNPKKNS SLKKTIQDAK KVLIPDNYIK 

       370        380        390        400        410        420 
RVIDLARQGY KEILFEELTT DWQSDAYNTV SGQNSNNSIR LTNEFMAAVE QDQPWNLYFR 

       430        440        450        460        470        480 
TEKEKAKVEG RKAKPSQTLR ARELWEKISY AAWASADPGT QYHTTINEWH TCPEDGPINA 

       490        500        510        520        530        540 
SNPCSEYMFL DNTACNLASA NLQKFVNLET LNFDVEGFRY LCKLWTIILE ISVTMAQFPS 

       550        560        570        580        590        600 
KEIAELSYKF RTLGLGYANL GSVLMVLGIP YDSQQAMAIT GAISSIMHMT AYATSAEMAK 

       610        620        630        640        650        660 
EQGPFVGYAK NQKHMLRVIR NHRRAAYNAP SGDYEGLTIT PIGINPAFCP SYMLKAAQED 

       670        680        690        700        710        720 
ADLALSLGEK YGFRNAQVTV IAPTGTIGLV MDCDTTGIEP DFALVKFKKL AGGGYFKIIN 

       730        740        750        760        770        780 
QSVPYGLKKL GYSPSEIEAI VNYCKGHATL NGAPVINTQA LKEKGFTNEI LEKVEASLPL 

       790        800        810        820        830        840 
AFDINFAFNK FNLGENFLTK NLGISKEIFD SPGFSLLEHL GFTKEDINKA NDYVCGTMTI 

       850        860        870        880        890        900 
ENAPFLKEKD YPVFDCANKC GKYGKRFLSY ESHIRIMAAA QPFISGAISK TINLPEEAVI 

       910        920        930        940        950        960 
EDIKNAYFLS WKMMIKANAL YRDGSKLSQP LNSVLELLNG IEIDDQEEIR EATISKDPVQ 

       970        980        990       1000       1010       1020 
IAEKIVTKYI SHRRKLPSRR AGYTQKAIVG GHKVYLRTGE YEDGQIGEIF IDMHKEGAAF 

      1030       1040       1050       1060       1070       1080 
RSLMNAFAIS VSLGLQHGVP LEEYVDAFTF FKFEPNGIVS GNKHIKMSTS VIDYIFRELA 

      1090       1100       1110       1120       1130       1140 
ITYLGRYDLG QVAPEDLRGD EIGSKRATAE SNGQEKETLS SMTAVIEPTP KKEVETISYS 

      1150       1160       1170       1180       1190       1200 
QMISKEKPSS SPSGISLLEE VKLAKIKGYT GDSCSECGSF EMVRNGSCLK CMSCGSTTGC 


S 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016823 Genomic DNA. Translation: AAS70183.1. Different initiation.
RefSeqYP_001546.1. NC_005823.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267671.LIC11587.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS70183; AAS70183; LIC_11587.
GeneID2772842.
KEGGlic:LIC11587.
PATRIC22375523. VBILepInt6257_1927.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00525.
OrthoDBEOG6H4K5F.

Enzyme and pathway databases

BioCycLINT267671:GHQI-1584-MONOMER.

Family and domain databases

InterProIPR013678. RNR_2_N.
IPR000788. RNR_lg_C.
IPR013344. RNR_NrdJ/NrdZ.
IPR024434. TSCPD_dom.
IPR029072. YebC-like.
[Graphical view]
PfamPF08471. Ribonuc_red_2_N. 1 hit.
PF02867. Ribonuc_red_lgC. 2 hits.
PF12637. TSCPD. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
SUPFAMSSF75625. SSF75625. 1 hit.
TIGRFAMsTIGR02504. NrdJ_Z. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNRDJ_LEPIC
AccessionPrimary (citable) accession number: Q72S00
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: August 10, 2010
Last modified: June 11, 2014
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families