NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
PubMed=12125824 [NCBI, ExPASy, EBI, Israel, Japan]
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.;
"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.";
J. Mol. Microbiol. Biotechnol. 4:453-461(2002).

Comments

CATALYTIC ACTIVITY: ATP + deamido-NAD⁺ + NH₃ = AMP + diphosphate + NAD⁺.
PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1 .
SIMILARITY: Belongs to the NAD synthetase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE008384; AAM30142.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_632470.1; -.

3D structure databases

HSSP

P08164; 1IFX. [HSSP ENTRY / PDB]

ModBase

Q8PZP6.

Enzyme and pathway databases

BioCyc

MMAZ192952:MM0446-MON; -.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0003952;	Molecular function: NAD+ synthase (glutamine-hydrolyzing) activity (inferred from electronic annotation from InterPro).
GO:0008795;	Molecular function: NAD+ synthase activity (inferred from electronic annotation from EC).
GO:0009435;	Biological process: NAD biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00193; -; 1.
PBIL [Tree]

InterPro

IPR003694; NAD_synthase.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.

Pfam

PF02540; NAD_synthase; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00552; nadE; 1.

ProtoNet

Q8PZP6.

Genome annotation databases

GeneID

1478788; -.

GenomeReviews

AE008384_GR; MM_0446.

KEGG

mma:MM_0446; -.

NMPDR

fig|192952.1.peg.446; -.

Phylogenomic databases

HOGENOM

Q8PZP6; -.

Genome annotation databases

CMR

Q8PZP6; MM_0446.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Complete proteome; Ligase; NAD; Nucleotide-binding.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 256`	`256`	`NH(3)-dependent NAD(+) synthetase.`	`PRO_0000152226`
`NP_BIND`	`29 36`	`8`	`ATP (By similarity).`
`ACT_SITE`	`31 31`		`By similarity.`

Sequence information

Length: 256 AA [This is the length of the unprocessed precursor]

Molecular weight: 27786 Da [This is the MW of the unprocessed precursor]

CRC64: 679195AE15E1D9C9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDLENAQNRI IDFIRDETGR AGVKGVVVGI SGGIDSALTA TLAVKALGKD RVLGIHMPES 

        70         80         90        100        110        120 
SLTPAVDSED AEALADWLGI EYRTIDISGI ISAFMAAVPE SESADRLTKG NLKARTRMSL 

       130        140        150        160        170        180 
LYFHANRLNR MVIGTGNKTE ILLGYYTKYG DGGVDLEPIG GLYKTGVWEL SSRLGIPESL 

       190        200        210        220        230        240 
ITKKPSAGLW AGQTDEADLG ISYVKVDEVL KMIEDGVEPE VILDKTGISA DQLNSVTRRI 

       250 
ERNEHKRKAP PVPELY

Q8PZP6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools