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Protein

Bifunctional NMN adenylyltransferase/Nudix hydrolase

Gene

slr0787

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The Nudix hydrolase domain is active on ADP-ribose, (2')-phospho-ADP-ribose, IDP-ribose and NADPH.

Catalytic activityi

ATP + nicotinamide ribonucleotide = diphosphate + NAD+.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes NAD(+) from nicotinamide D-ribonucleotide.
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional NMN adenylyltransferase/Nudix hydrolase (slr0787)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes NAD(+) from nicotinamide D-ribonucleotide, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, NAD, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8321.
BRENDAi2.7.7.1. 382.
3.6.1.13. 382.
UniPathwayiUPA00253; UER00600.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional NMN adenylyltransferase/Nudix hydrolase
Including the following 2 domains:
Nicotinamide-nucleotide adenylyltransferase (EC:2.7.7.1)
Alternative name(s):
NAD(+) diphosphorylase
NAD(+) pyrophosphorylase
NMN adenylyltransferase
ADP compounds hydrolase (EC:3.6.1.-)
Gene namesi
Ordered Locus Names:slr0787
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 339339Bifunctional NMN adenylyltransferase/Nudix hydrolasePRO_0000135011Add
BLAST

Interactioni

Protein-protein interaction databases

DIPiDIP-29582N.
IntActiQ55928. 3 interactions.

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1211Combined sources
Helixi19 – 3113Combined sources
Beta strandi32 – 4211Combined sources
Beta strandi48 – 503Combined sources
Helixi54 – 629Combined sources
Helixi67 – 704Combined sources
Beta strandi73 – 797Combined sources
Helixi85 – 10016Combined sources
Beta strandi106 – 1105Combined sources
Helixi115 – 1217Combined sources
Beta strandi126 – 1305Combined sources
Helixi139 – 14810Combined sources
Helixi151 – 1533Combined sources
Turni154 – 1574Combined sources
Helixi160 – 16910Combined sources
Helixi173 – 19018Combined sources
Turni191 – 1944Combined sources
Beta strandi195 – 1973Combined sources
Beta strandi201 – 21010Combined sources
Beta strandi213 – 2186Combined sources
Beta strandi221 – 2244Combined sources
Beta strandi231 – 2344Combined sources
Helixi241 – 25313Combined sources
Helixi259 – 2646Combined sources
Beta strandi266 – 2727Combined sources
Beta strandi283 – 2919Combined sources
Beta strandi294 – 2963Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi309 – 3135Combined sources
Helixi314 – 3196Combined sources
Helixi321 – 3233Combined sources
Helixi328 – 3358Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QJOX-ray2.60A/B/C1-339[»]
ProteinModelPortaliQ55928.
SMRiQ55928. Positions 4-339.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ55928.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini199 – 335137Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 183183NMN adenylyltransferaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi233 – 25422Nudix boxAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the archaeal NMN adenylyltransferase family.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiQ55928.
KOiK13522.
OMAiYPPVFVT.
OrthoDBiEOG632D2F.
PhylomeDBiQ55928.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.90.79.10. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_like. 1 hit.
PF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q55928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTKYQYGIY IGRFQPFHLG HLRTLNLALE KAEQVIIILG SHRVAADTRN
60 70 80 90 100
PWRSPERMAM IEACLSPQIL KRVHFLTVRD WLYSDNLWLA AVQQQVLKIT
110 120 130 140 150
GGSNSVVVLG HRKDASSYYL NLFPQWDYLE TGHYPDFSST AIRGAYFEGK
160 170 180 190 200
EGDYLDKVPP AIADYLQTFQ KSERYIALCD EYQFLQAYKQ AWATAPYAPT
210 220 230 240 250
FITTDAVVVQ AGHVLMVRRQ AKPGLGLIAL PGGFIKQNET LVEGMLRELK
260 270 280 290 300
EETRLKVPLP VLRGSIVDSH VFDAPGRSLR GRTITHAYFI QLPGGELPAV
310 320 330
KGGDDAQKAW WMSLADLYAQ EEQIYEDHFQ IIQHFVSKV
Length:339
Mass (Da):38,532
Last modified:November 1, 1996 - v1
Checksum:iB12938EBE97465BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10693.1.
PIRiS77001.

Genome annotation databases

EnsemblBacteriaiBAA10693; BAA10693; BAA10693.
KEGGisyn:slr0787.
PATRICi23842984. VBISynSp132158_3030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10693.1.
PIRiS77001.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QJOX-ray2.60A/B/C1-339[»]
ProteinModelPortaliQ55928.
SMRiQ55928. Positions 4-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29582N.
IntActiQ55928. 3 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA10693; BAA10693; BAA10693.
KEGGisyn:slr0787.
PATRICi23842984. VBISynSp132158_3030.

Phylogenomic databases

InParanoidiQ55928.
KOiK13522.
OMAiYPPVFVT.
OrthoDBiEOG632D2F.
PhylomeDBiQ55928.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00600.
BioCyciMetaCyc:MONOMER-8321.
BRENDAi2.7.7.1. 382.
3.6.1.13. 382.

Miscellaneous databases

EvolutionaryTraceiQ55928.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.90.79.10. 1 hit.
InterProiIPR004821. Cyt_trans-like.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_like. 1 hit.
PF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
    Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
    DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27184 / PCC 6803 / N-1.
  2. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
    Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.
  3. "Synechocystis sp. slr0787 protein is a novel bifunctional enzyme endowed with both nicotinamide mononucleotide adenylyltransferase and 'Nudix' hydrolase activities."
    Raffaelli N., Lorenzi T., Amici A., Emanuelli M., Ruggieri S., Magni G.
    FEBS Lett. 444:222-226(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiNADM_SYNY3
AccessioniPrimary (citable) accession number: Q55928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: March 16, 2016
This is version 128 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

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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 one 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.