Reviewed, UniProtKB/Swiss-Prot Q9ZLF9 (RIR1_HELPJ)

Names and origin

Protein names

Recommended name:
    Ribonucleoside-diphosphate reductase subunit alpha
    EC=1.17.4.1
Alternative name(s):
    Ribonucleotide reductase

Gene names

Name:	nrdA
Ordered Locus Names:	jhp_0621

Organism

Helicobacter pylori J99 (Campylobacter pylori J99) [Complete proteome] [HAMAP]

Taxonomic identifier

85963 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	788 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity.
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Tetramer of two alpha and two beta subunits By similarity.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase large chain family. Contains 1 ATP-cone domain.

Ontologies

Keywords
Biological process	DNA replication
Ligand	ATP-binding Nucleotide-binding
Molecular function	Oxidoreductase
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro ribonucleoside-diphosphate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 788	788	Ribonucleoside-diphosphate reductase subunit alpha		PRO_0000187216
Regions
	Domain	2 – 92	91	ATP-cone
Sites
	Active site	216	1	Hydrogen atom transfer By similarity
	Active site	424	1	Proton acceptor By similarity
	Active site	426	1	Proton acceptor By similarity
	Active site	428	1	Proton acceptor By similarity
	Active site	497	1	Hydrogen atom transfer By similarity
	Active site	763	1	Electron transfer By similarity
	Active site	764	1	Electron transfer By similarity
	Site	223	1	Allosteric effector binding By similarity
	Site	253	1	Allosteric effector binding By similarity
	Site	784	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	787	1	Interacts with thioredoxin/glutaredoxin By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9ZLF9-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: A98AFCBC5CC6398E	FASTA	788	90,232
	10 20 30 40 50 60 MITVVKRNGR IEPLDITKIQ KYTKDATDNL EGVSQSELEV DARLQFRDKI TTEEIQQTLI 70 80 90 100 110 120 KTAVDKIDID TPNWSFVASR LFLYDLYHKV SGFTGYRHLK EYFENAEEKG RILKGFKEKF 130 140 150 160 170 180 DLEFLNSQIK PERDFQFNYL GIKTLYDRYL LKDANNHPIE LPQHMFMSIA MFLAQNEQEL 190 200 210 220 230 240 NKIALEFYEV LSKFEAMCAT PTLANARTTK HQLSSCYIGS TPDNIEGIFD SYKEMALLSK 250 260 270 280 290 300 YGGGIGWDFS LVRSIGSYID GHKNASAGTI PFLKIANDVA IAVDQLGTRK GAIAVYLEIW 310 320 330 340 350 360 HIDVMEFIDL RKNSGDERRR AHDLFPALWV CDLFMKRVLE DAMWTLFDPY ECKDLTELYG 370 380 390 400 410 420 QDFEKRYLEY EKDPKIIKEY INAKDLWKKI LMNYFEAGLP FLAFKDNANR CNPNAHAGII 430 440 450 460 470 480 RSSNLCTEIF QNTAPNHYYM QIEYTDGAIE FFEEKELVTT DSNITKCANK LTSTDILKGK 490 500 510 520 530 540 KIYIATKVAK DGQTAVCNLA SINLSKINTE EDIKRVVPIM VRLLDNVIDL NFYPNRKVKA 550 560 570 580 590 600 TNLQNRAIGL GVMGEAQMLA EHQIAWGSKE HLEKIDALME QISYHAIDTS ANLAKEKGVY 610 620 630 640 650 660 KDFENSEWSK GIFPIDKANN EALKLTEKGL FNHACDWQGL REKVKANGMR NGYLMAIAPT 670 680 690 700 710 720 SSISILVGTT QTIEPIYKKK WFEENLSGLI PVVVPNLNVE TWNFYTSAYD IDAKDLIKAA 730 740 750 760 770 780 AVRQKWIDQG QSINVFLRIE NASGKTLHEI YTLAWKLGLK STYYLRSESP SIDEKSVLDR SVECFNCQ

References

[1]

"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori." Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J. Nature 397:176-180(1999) [PubMed: 9923682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE001439 Genomic DNA. Translation: AAD06201.1.
PIR	F71908.
RefSeq	NP_223339.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9ZLF9.
Genome annotation databases
GeneID	890291.
GenomeReviews	Gene locus jhp_0621 in contig AE001439_GR.
KEGG	hpj:jhp0621.
NMPDR	fig|85963.1.peg.617.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9ZLF9.
OMA	RHVDQSI.
Enzyme and pathway databases
BioCyc	HPYL85963:JHP0621-MON.
BRENDA	1.17.4.1. 295085.
Family and domain databases
InterPro	IPR005144. ATP-cone. IPR013346. NrdE_NrdA. IPR013509. Ribncl_Rdtase_lsu_N. IPR000788. Ribncl_red_lg_C. [Graphical view]
PANTHER	PTHR11573. Ribncl_red_lg_C. 1 hit.
Pfam	PF03477. ATP-cone. 1 hit. PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. [Graphical view]
PRINTS	PR01183. RIBORDTASEM1.
TIGRFAMs	TIGR02506. NrdE_NrdA. 1 hit.
PROSITE	PS51161. ATP_CONE. 1 hit. PS00089. RIBORED_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR1_HELPJ

Accession

Primary (citable) accession number: Q9ZLF9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)