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Q5R919

- RIR1_PONAB

UniProt

Q5R919 - RIR1_PONAB

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Protein
Ribonucleoside-diphosphate reductase large subunit
Gene
RRM1
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides 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 to separate specificity and activation sites on the M1 subunit. 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. Stimulated by ATP and inhibited by dATP binding to the activity site By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei5 – 51Allosteric activator By similarity
Binding sitei53 – 531Allosteric activator By similarity
Binding sitei88 – 881Allosteric activator By similarity
Binding sitei202 – 2021Substrate By similarity
Sitei218 – 2181Important for hydrogen atom transfer By similarity
Sitei226 – 2261Allosteric effector binding, determines substrate specificity By similarity
Binding sitei247 – 2471Substrate; via amide nitrogen By similarity
Sitei256 – 2561Allosteric effector binding, determines substrate specificity By similarity
Active sitei427 – 4271Proton acceptor By similarity
Active sitei429 – 4291Cysteine radical intermediate By similarity
Active sitei431 – 4311Proton acceptor By similarity
Sitei444 – 4441Important for hydrogen atom transfer By similarity
Sitei737 – 7371Important for electron transfer By similarity
Sitei738 – 7381Important for electron transfer By similarity
Sitei787 – 7871Interacts with thioredoxin/glutaredoxin By similarity
Sitei790 – 7901Interacts with thioredoxin/glutaredoxin By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. DNA replication Source: UniProtKB-UniPathway
  2. deoxyribonucleotide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
Alternative name(s):
Ribonucleoside-diphosphate reductase subunit M1
Ribonucleotide reductase large subunit
Gene namesi
Name:RRM1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. ribonucleoside-diphosphate reductase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 792792Ribonucleoside-diphosphate reductase large subunit
PRO_0000290352Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171N6-acetyllysine By similarity
Disulfide bondi218 ↔ 444Redox-active By similarity
Modified residuei376 – 3761N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PRIDEiQ5R919.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit. Interacts with RRM2B By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5R919.
SMRiQ5R919. Positions 15-759.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9292ATP-cone
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 177Allosteric activator binding By similarity
Regioni217 – 2182Substrate binding By similarity
Regioni285 – 2884Allosteric effector binding, determines substrate specificity By similarity
Regioni427 – 4315Substrate binding By similarity
Regioni603 – 6075Substrate binding By similarity

Sequence similaritiesi

Contains 1 ATP-cone domain.

Phylogenomic databases

HOVERGENiHBG003447.
InParanoidiQ5R919.
KOiK10807.

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.

Q5R919-1 [UniParc]FASTAAdd to Basket

« Hide

MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG    50
VTTVELDTLA AETAATLTTK HPDYAILAAR IAVSNLHKEA KKVFSDVMED 100
LYNYINPHNG KHSPMVAKST LDIVLANKDR LNSAIIYDRD FSYNYFGFKT 150
LERSYLLKIN GKVAERPQHM LMRVSVGIHK EDIDAAIETY NLLSERWFTH 200
ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL ISKSAGGIGV 250
AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY 300
LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL 350
MCPNECPGLD EVWGEEFEKL YASYEKQGRV RKVVKAQQLW YAIIESQTET 400
GTPYMLYKDS CNRKSNQQNL GTIKCSSLCT EIVEYTSKDE VAVCNLASLA 450
LNMYVTSEHT YDFKKLAEVT KVVVRNLNKI IDINYYPVPE ACLSNKRHRP 500
IGIGVQGLAD AFILMRYPFE SAEAQLLNKQ IFETIYYGAL EASCDLAKEQ 550
GPYETYEGSP VSKGILQYDM WNVTPTDLWD WKLLKEKIAK YGIRNSLLIA 600
PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL 650
WHEEMKNQII ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA 700
FIDQSQSLNI HIAEPNYGKL TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF 750
TLNKEKLKDK EKVSKEEEEK ERNTAAMVCS LENRDECLMC GS 792
Length:792
Mass (Da):90,027
Last modified:December 21, 2004 - v1
Checksum:i93AC48CB6CEEC044
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859577 mRNA. Translation: CAH91741.1.
RefSeqiNP_001126012.1. NM_001132540.2.
UniGeneiPab.9179.

Genome annotation databases

GeneIDi100172956.
KEGGipon:100172956.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859577 mRNA. Translation: CAH91741.1 .
RefSeqi NP_001126012.1. NM_001132540.2.
UniGenei Pab.9179.

3D structure databases

ProteinModelPortali Q5R919.
SMRi Q5R919. Positions 15-759.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q5R919.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100172956.
KEGGi pon:100172956.

Organism-specific databases

CTDi 6240.

Phylogenomic databases

HOVERGENi HBG003447.
InParanoidi Q5R919.
KOi K10807.

Enzyme and pathway databases

UniPathwayi UPA00326 .

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. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.

Entry informationi

Entry nameiRIR1_PONAB
AccessioniPrimary (citable) accession number: Q5R919
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: December 21, 2004
Last modified: October 16, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Two distinct regulatory sites have been defined: the specificity site, which controls substrate specificity, and the activity site which regulates overall catalytic activity. A substrate-binding catalytic site, located on M1, is formed only in the presence of the second subunit M2 By similarity.

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

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