O26253 (NADM_METTH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nicotinamide-nucleotide adenylyltransferase
EC=2.7.7.1

Alternative name(s):
NAD(+) diphosphorylase
NAD(+) pyrophosphorylase
NMN adenylyltransferase

Gene names

Ordered Locus Names:

MTH_150

Organism

Methanobacterium thermoautotrophicum (strain Delta H)

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	178 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + nicotinamide ribonucleotide = diphosphate + NAD+. HAMAP MF_00243
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1. HAMAP MF_00243
Subunit structure	Homohexamer.
Subcellular location	Cytoplasm By similarity HAMAP MF_00243.
Sequence similarities	Belongs to the archaeal NMN adenylyltransferase family.
Sequence caution	The sequence AAB84656.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding NAD Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	NAD biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nicotinamide-nucleotide adenylyltransferase 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 – 178

178

Nicotinamide-nucleotide adenylyltransferase HAMAP MF_00243

PRO_0000134995

Secondary structure

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178

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Helix

14 – 23

10

Turn

24 – 26

3

Beta strand

28 – 34

7

Beta strand

41 – 45

5

Helix

49 – 62

14

Helix

67 – 69

3

Beta strand

70 – 74

5

Helix

81 – 91

11

Beta strand

96 – 99

4

Helix

103 – 111

9

Turn

124 – 126

3

Helix

129 – 138

10

Helix

143 – 145

3

Helix

148 – 156

9

Helix

159 – 166

8

Sequences

	Sequence		Length	Mass (Da)
	O26253 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: A1B4F41BA3FF98AE	FASTA	178	20,207
	10 20 30 40 50 60 MRGLLVGRMQ PFHRGHLQVI KSILEEVDEL IICIGSAQLS HSIRDPFTAG ERVMMLTKAL 70 80 90 100 110 120 SENGIPASRY YIIPVQDIEC NALWVGHIKM LTPPFDRVYS GNPLVQRLFS EDGYEVTAPP 130 140 150 160 170 LFYRDRYSGT EVRRRMLDDG DWRSLLPESV VEVIDEINGV ERIKHLAKKE VSELGGIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N. J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Delta H.
[2]	"Structural proteomics of an archaeon." Christendat D., Yee A., Dharamsi A., Kluger Y., Savchenko A., Cort J.R., Booth V., Mackereth C.D., Saridakis V., Ekiel I., Kozlov G., Maxwell K.L., Wu N., McIntosh L.P., Gehring K., Kennedy M.A., Davidson A.R., Pai E.F. , Gerstein M., Edwards A.M., Arrowsmith C.H. Nat. Struct. Biol. 7:903-909(2000) [PubMed: 11017201] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000666 Genomic DNA. Translation: AAB84656.1. Different initiation.

PIR

A69067.

RefSeq

NP_275293.1. NC_000916.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EJ2	X-ray	1.90	A	1-178	[»]
1HYB	X-ray	2.00	A	1-178	[»]
1M8F	X-ray	2.40	A	1-178	[»]
1M8G	X-ray	2.00	A	1-178	[»]
1M8J	X-ray	2.40	A	1-178	[»]
1M8K	X-ray	3.00	A/B/C	1-178	[»]

ProteinModelPortal

O26253.

SMR

O26253. Positions 1-167.

ModBase

Search...

Protein-protein interaction databases

STRING

O26253.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1470111.

GenomeReviews

Gene locus MTH_150 in contig AE000666_GR.

KEGG

mth:MTH150.

NMPDR

fig|187420.1.peg.148.

Phylogenomic databases

eggNOG

arNOG10577.

HOGENOM

HBG392019.

OMA

FHKGHLE.

ProtClustDB

PRK01153.

Enzyme and pathway databases

BioCyc

MTHE187420:MTH150-MONOMER.

Family and domain databases

HAMAP

MF_00243. NMN_adenylyltr.
[Tree]

InterPro

IPR004821. Cyt_trans-rel.
IPR004820. Cytidylyltransf.
IPR006418. NMN_Atrans_arc.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Gene3D

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

KO

K00952.

Pfam

PF01467. CTP_transf_2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01527. Arch_NMN_Atrans. 1 hit.
TIGR00125. Cyt_tran_rel. 1 hit.

ProtoNet

Search...

Entry information

Entry name

NADM_METTH

Accession

Primary (citable) accession number: O26253

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	November 16, 2011
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program