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Protein

Vitamin B12-dependent ribonucleotide reductase

Gene

nrdJ

Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

adenosylcob(III)alaminBy similarityNote: 5'-deoxyadenosylcobalamine (coenzyme B12).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei153 – 1531SubstrateBy similarity
Binding sitei230 – 2301Substrate; via amide nitrogenBy similarity
Active sitei482 – 4821Proton acceptorBy similarity
Active sitei484 – 4841Cysteine radical intermediateBy similarity
Active sitei486 – 4861Proton acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA synthesis

Keywords - Ligandi

Cobalamin, Cobalt, Nucleotide-binding

Enzyme and pathway databases

BioCyciLINT267671:GHQI-1584-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin B12-dependent ribonucleotide reductase (EC:1.17.4.1)
Alternative name(s):
Ribonucleoside-diphosphate reductase NrdJ
Gene namesi
Name:nrdJ
Ordered Locus Names:LIC_11587
OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Taxonomic identifieri267671 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesLeptospiralesLeptospiraceaeLeptospira
ProteomesiUP000007037 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12011201Vitamin B12-dependent ribonucleotide reductasePRO_0000231659Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi199 ↔ 495Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi267671.LIC11587.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 1992Substrate bindingBy similarity
Regioni482 – 4865Substrate bindingBy similarity
Regioni683 – 6875Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

KOiK00525.
OrthoDBiEOG6H4K5F.

Family and domain databases

InterProiIPR013678. RNR_2_N.
IPR000788. RNR_lg_C.
IPR013344. RNR_NrdJ/NrdZ.
IPR024434. TSCPD_dom.
IPR029072. YebC-like.
[Graphical view]
PfamiPF08471. Ribonuc_red_2_N. 1 hit.
PF02867. Ribonuc_red_lgC. 2 hits.
PF12637. TSCPD. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF75625. SSF75625. 1 hit.
TIGRFAMsiTIGR02504. NrdJ_Z. 1 hit.

Sequencei

Sequence statusi: Complete.

Q72S00-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMNRHFTVP QNGESSTIQW TKRNSKITNP DGSKVFEAND ILVPEDWSQV
60 70 80 90 100
AVDILAQKYF RRKGVPKYLK KVQEDGIPEW LQKSIPDTEK LESLKPEDRF
110 120 130 140 150
GGETSALEVF HRLAGCWTYW GYKYKYFSDE ESAKIFYDEI VYMLATQMAA
160 170 180 190 200
PNSPQWFNTG LNWAYGIDGK SQGHYYVDPS TGKLVKSTSA YEHPQPHACF
210 220 230 240 250
IQSVDDDLVN EGGIMDLWVR EARLFKYGSG TGTNFSNLRG ENEPLSGGGK
260 270 280 290 300
SSGLMSFLKI GDRAAGAIKS GGTTRRAAKM VCLDVDHPDI ENFIDWKVTE
310 320 330 340 350
EKKVASLVTG SMLNNRHLNA IMSACYEMEG EDRFNPKKNS SLKKTIQDAK
360 370 380 390 400
KVLIPDNYIK RVIDLARQGY KEILFEELTT DWQSDAYNTV SGQNSNNSIR
410 420 430 440 450
LTNEFMAAVE QDQPWNLYFR TEKEKAKVEG RKAKPSQTLR ARELWEKISY
460 470 480 490 500
AAWASADPGT QYHTTINEWH TCPEDGPINA SNPCSEYMFL DNTACNLASA
510 520 530 540 550
NLQKFVNLET LNFDVEGFRY LCKLWTIILE ISVTMAQFPS KEIAELSYKF
560 570 580 590 600
RTLGLGYANL GSVLMVLGIP YDSQQAMAIT GAISSIMHMT AYATSAEMAK
610 620 630 640 650
EQGPFVGYAK NQKHMLRVIR NHRRAAYNAP SGDYEGLTIT PIGINPAFCP
660 670 680 690 700
SYMLKAAQED ADLALSLGEK YGFRNAQVTV IAPTGTIGLV MDCDTTGIEP
710 720 730 740 750
DFALVKFKKL AGGGYFKIIN QSVPYGLKKL GYSPSEIEAI VNYCKGHATL
760 770 780 790 800
NGAPVINTQA LKEKGFTNEI LEKVEASLPL AFDINFAFNK FNLGENFLTK
810 820 830 840 850
NLGISKEIFD SPGFSLLEHL GFTKEDINKA NDYVCGTMTI ENAPFLKEKD
860 870 880 890 900
YPVFDCANKC GKYGKRFLSY ESHIRIMAAA QPFISGAISK TINLPEEAVI
910 920 930 940 950
EDIKNAYFLS WKMMIKANAL YRDGSKLSQP LNSVLELLNG IEIDDQEEIR
960 970 980 990 1000
EATISKDPVQ IAEKIVTKYI SHRRKLPSRR AGYTQKAIVG GHKVYLRTGE
1010 1020 1030 1040 1050
YEDGQIGEIF IDMHKEGAAF RSLMNAFAIS VSLGLQHGVP LEEYVDAFTF
1060 1070 1080 1090 1100
FKFEPNGIVS GNKHIKMSTS VIDYIFRELA ITYLGRYDLG QVAPEDLRGD
1110 1120 1130 1140 1150
EIGSKRATAE SNGQEKETLS SMTAVIEPTP KKEVETISYS QMISKEKPSS
1160 1170 1180 1190 1200
SPSGISLLEE VKLAKIKGYT GDSCSECGSF EMVRNGSCLK CMSCGSTTGC

S
Length:1,201
Mass (Da):133,918
Last modified:August 10, 2010 - v2
Checksum:i062F88B39A9A120C
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016823 Genomic DNA. Translation: AAS70183.1. Different initiation.
RefSeqiWP_011172208.1. NC_005823.1.
YP_001546.1. NC_005823.1.

Genome annotation databases

EnsemblBacteriaiAAS70183; AAS70183; LIC_11587.
KEGGilic:LIC11587.
PATRICi22375523. VBILepInt6257_1927.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016823 Genomic DNA. Translation: AAS70183.1. Different initiation.
RefSeqiWP_011172208.1. NC_005823.1.
YP_001546.1. NC_005823.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi267671.LIC11587.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS70183; AAS70183; LIC_11587.
KEGGilic:LIC11587.
PATRICi22375523. VBILepInt6257_1927.

Phylogenomic databases

KOiK00525.
OrthoDBiEOG6H4K5F.

Enzyme and pathway databases

BioCyciLINT267671:GHQI-1584-MONOMER.

Family and domain databases

InterProiIPR013678. RNR_2_N.
IPR000788. RNR_lg_C.
IPR013344. RNR_NrdJ/NrdZ.
IPR024434. TSCPD_dom.
IPR029072. YebC-like.
[Graphical view]
PfamiPF08471. Ribonuc_red_2_N. 1 hit.
PF02867. Ribonuc_red_lgC. 2 hits.
PF12637. TSCPD. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF75625. SSF75625. 1 hit.
TIGRFAMsiTIGR02504. NrdJ_Z. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis."
    Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S.
    , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.
    J. Bacteriol. 186:2164-2172(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Fiocruz L1-130.

Entry informationi

Entry nameiNRDJ_LEPIC
AccessioniPrimary (citable) accession number: Q72S00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: August 10, 2010
Last modified: June 24, 2015
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.