Nicotinate-nucleotide adenylyltransferase - Escherichia coli (strain K12)

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P0A752 (NADD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Nicotinate-nucleotide adenylyltransferase
EC=2.7.7.18

Alternative name(s):
Deamido-NAD(+) diphosphorylase
Deamido-NAD(+) pyrophosphorylase
Nicotinate mononucleotide adenylyltransferase
Short name=NaMN adenylyltransferase

Gene names

Name:	nadD
Synonyms:	ybeN
Ordered Locus Names:	b0639, JW0634

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). HAMAP-Rule MF_00244
Catalytic activity	ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD⁺. HAMAP-Rule MF_00244
Enzyme regulation	Activity is susceptible to product inhibition. HAMAP-Rule MF_00244
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. HAMAP-Rule MF_00244
Sequence similarities	Belongs to the NadD family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Ligand	ATP-binding NAD Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NAD salvage Inferred from mutant phenotype PubMed 12949168. Source: EcoCyc de novo NAD biosynthetic process from aspartate Inferred from mutant phenotype PubMed 12949168. Source: EcoCyc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nicotinate-nucleotide adenylyltransferase activity Inferred from direct assay Ref.7. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 213

213

Nicotinate-nucleotide adenylyltransferase HAMAP-Rule MF_00244

PRO_0000181407

Secondary structure

213

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A752 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: EA2C675282400CF5
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FASTA

213

24,528

        10         20         30         40         50         60 
MKSLQALFGG TFDPVHYGHL KPVETLANLI GLTRVTIIPN NVPPHRPQPE ANSVQRKHML 

        70         80         90        100        110        120 
ELAIADKPLF TLDERELKRN APSYTAQTLK EWRQEQGPDV PLAFIIGQDS LLTFPTWYEY 

       130        140        150        160        170        180 
ETILDNAHLI VCRRPGYPLE MAQPQYQQWL EDHLTHNPED LHLQPAGKIY LAETPWFNIS 

       190        200        210 
ATIIRERLQN GESCEDLLPE PVLTYINQQG LYR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Addinall S.G., Donachie W.D. Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography." Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B. Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: B / BL21.
[7]	"Identification of the Escherichia coli nicotinic acid mononucleotide adenylyltransferase gene." Mehl R.A., Kinsland C., Begley T.P. J. Bacteriol. 182:4372-4374(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: B.
[8]	"Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD." Zhang H., Zhou T., Kurnasov O., Cheek S., Grishin N.V., Osterman A. Structure 10:69-79(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U23163 Genomic DNA. Translation: AAA64852.1.
U82598 Genomic DNA. Translation: AAB40840.1.
U00096 Genomic DNA. Translation: AAC73740.1.
AP009048 Genomic DNA. Translation: BAA35286.1.

PIR

E64798.

RefSeq

NP_415172.1. NC_000913.2.
YP_488930.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K4K	X-ray	2.00	A/B/C/D	1-213	[»]
1K4M	X-ray	1.90	A/B/C	1-213	[»]

ProteinModelPortal

P0A752.

SMR

P0A752. Positions 1-213.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A752. 7 interactions.

STRING

511145.b0639.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73740; AAC73740; b0639.
BAA35286; BAA35286; BAA35286.

GeneID

12932665.
945248.

KEGG

ecj:Y75_p0629.
eco:b0639.

PATRIC

32116461. VBIEscCol129921_0670.

Organism-specific databases

EchoBASE

EB3030.

EcoGene

EG13241. nadD.

Phylogenomic databases

eggNOG

COG1057.

HOGENOM

HOG000262781.

K00969.

OMA

HYGHLRP.

ProtClustDB

PRK00071.

Enzyme and pathway databases

BioCyc

EcoCyc:NICONUCADENYLYLTRAN-MONOMER.
ECOL316407:JW0634-MONOMER.
MetaCyc:NICONUCADENYLYLTRAN-MONOMER.

UniPathway

UPA00253; UER00332.

Gene expression databases

Genevestigator

P0A752.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

HAMAP

MF_00244. NaMN_adenylyltr.

InterPro

IPR004821. Cyt_trans-like.
IPR005248. NAMN_adtrnsfrase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

PANTHER

PTHR12039. PTHR12039. 1 hit.

Pfam

PF01467. CTP_transf_2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00125. cyt_tran_rel. 1 hit.
TIGR00482. TIGR00482. 1 hit.

ProtoNet

Search...

Other

BindingDB

P0A752.

EvolutionaryTrace

P0A752.

Entry information

Entry name

NADD_ECOLI

Accession

Primary (citable) accession number: P0A752
Secondary accession number(s): P52085

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents