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O83972

- RIR1_TREPA

UniProt

O83972 - RIR1_TREPA

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Protein

Ribonucleoside-diphosphate reductase subunit alpha

Gene

nrdA

Organism
Treponema pallidum (strain Nichols)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).By similarity

Catalytic activityi

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

Enzyme regulationi

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction (By similarity).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei303 – 3031SubstrateBy similarity
Sitei319 – 3191Important for hydrogen atom transferBy similarity
Sitei326 – 3261Allosteric effector bindingBy similarity
Binding sitei347 – 3471Substrate; via amide nitrogenBy similarity
Sitei356 – 3561Allosteric effector bindingBy similarity
Active sitei534 – 5341Proton acceptorBy similarity
Active sitei536 – 5361Cysteine radical intermediateBy similarity
Active sitei538 – 5381Proton acceptorBy similarity
Sitei574 – 5741Important for hydrogen atom transferBy similarity
Sitei828 – 8281Important for electron transferBy similarity
Sitei829 – 8291Important for electron transferBy similarity
Sitei840 – 8401Interacts with thioredoxin/glutaredoxinBy similarity
Sitei843 – 8431Interacts with thioredoxin/glutaredoxinBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB-EC

GO - Biological processi

  1. DNA replication Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTPAL243276:GC1H-1063-MONOMER.
UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase subunit alpha (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase
Gene namesi
Name:nrdA
Ordered Locus Names:TP_1008
OrganismiTreponema pallidum (strain Nichols)
Taxonomic identifieri243276 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema
ProteomesiUP000000811: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 845845Ribonucleoside-diphosphate reductase subunit alphaPRO_0000187223Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi319 ↔ 574Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.By similarity

Protein-protein interaction databases

IntActiO83972. 2 interactions.
STRINGi243276.TP1008.

Structurei

3D structure databases

ProteinModelPortaliO83972.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9898ATP-conePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni318 – 3192Substrate bindingBy similarity
Regioni534 – 5385Substrate bindingBy similarity
Regioni725 – 7295Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 ATP-cone domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0209.
KOiK00525.
OMAiVSEASEY.
OrthoDBiEOG6J48HC.

Family and domain databases

InterProiIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamiPF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSiPR01183. RIBORDTASEM1.
SUPFAMiSSF48168. SSF48168. 1 hit.
TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
PROSITEiPS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O83972-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHIIKRNGEP QPYMREKIIV AISAAFRSVQ NPLAPEVPAI ITDLAAEVER
60 70 80 90 100
QLFEMNRAGV PVHVEKIQDF VEKTLTKYNH SDEVKSFILY RDDRTKKRIA
110 120 130 140 150
REQIACCFTD SSVLGVLKEI QQDFPFPEYS LDALASKFLL FKKEVTDERR
160 170 180 190 200
SMQLLIKAAV ELTAQEAPQW ELIAARLLML DFSLALGTSL EKLNIHSFYE
210 220 230 240 250
KITYLEEAGL YGVYIRTHYS RAEIEEAATY LECSRDKLFT YSSLDMILRR
260 270 280 290 300
YVIRTRAHVP LETPQEMFLG IALHLAMNET QDRMQWVKRF YTVLSKLQVT
310 320 330 340 350
VATPTLSNAR KPFHQLSSCF VDTVPDSLDG IYRSIDNFSQ VSKFGGGMGL
360 370 380 390 400
YFGKVRAVGA PIRGFQGAAG GILRWIKLAN DTAVAVDQLG VRQGSVAVYL
410 420 430 440 450
DVWHKDIPEF LQLRTNNGDD RMKAHDVFPA VCYPDLFWKT VRDNLGASWY
460 470 480 490 500
LMCPHEILTV KGYALEDFYA EEWEKRYWDC VKDARISKRT IPIKELVRLV
510 520 530 540 550
LKSVVETGTP FAFYRDHANR ANPNGHRGII YCSNLCTEIA QNMSAINLVS
560 570 580 590 600
VKITEVDGQK VVVQTTRPGD FVVCNLASLV LSNIDLSDDK ELREVVRVAV
610 620 630 640 650
RALDNVIDLT YYPVPYAQVT NAYYRAIGLG VSGYHHVLAQ QGIDWESDEH
660 670 680 690 700
LAFADRIFER INRAAIEASM TIAREKGAYG CFTGSDWCTG AYFRKRGYVS
710 720 730 740 750
EDWQRLQREV ATHGMRNGYL LAVAPTSSTS IIAGTTAGVD PIMKQYFLEE
760 770 780 790 800
KKGMLMPRVA PSLSQKTCPL YKSAHAVEQR WSIRAAGLRQ RHIDQAQSVN
810 820 830 840
LYITTDFTLK QVLDLYVYAW EVGMKSLYYV RSQSLEIDLC GYCAS
Length:845
Mass (Da):95,987
Last modified:November 1, 1998 - v1
Checksum:i47DC688E4D0B356C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000520 Genomic DNA. Translation: AAC65956.1.
PIRiB71255.
RefSeqiNP_219445.1. NC_000919.1.
YP_008091827.1. NC_021490.2.

Genome annotation databases

EnsemblBacteriaiAAC65956; AAC65956; TP_1008.
GeneIDi15852298.
2610819.
KEGGitpa:TP1008.
tpw:TPANIC_1008.
PATRICi20532141. VBITrePal57110_1063.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000520 Genomic DNA. Translation: AAC65956.1 .
PIRi B71255.
RefSeqi NP_219445.1. NC_000919.1.
YP_008091827.1. NC_021490.2.

3D structure databases

ProteinModelPortali O83972.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O83972. 2 interactions.
STRINGi 243276.TP1008.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC65956 ; AAC65956 ; TP_1008 .
GeneIDi 15852298.
2610819.
KEGGi tpa:TP1008.
tpw:TPANIC_1008.
PATRICi 20532141. VBITrePal57110_1063.

Phylogenomic databases

eggNOGi COG0209.
KOi K00525.
OMAi VSEASEY.
OrthoDBi EOG6J48HC.

Enzyme and pathway databases

UniPathwayi UPA00326 .
BioCyci TPAL243276:GC1H-1063-MONOMER.

Family and domain databases

InterProi IPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view ]
Pfami PF03477. ATP-cone. 1 hit.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view ]
PRINTSi PR01183. RIBORDTASEM1.
SUPFAMi SSF48168. SSF48168. 1 hit.
TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
PROSITEi PS51161. ATP_CONE. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Nichols.

Entry informationi

Entry nameiRIR1_TREPA
AccessioniPrimary (citable) accession number: O83972
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: October 29, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3