Q979C2 (RIBL_THEVO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
FAD synthase
EC=2.7.7.2

Alternative name(s):
FMN adenylyltransferase
Flavin adenine dinucleotide synthase

Gene names

Name:	ribL
Ordered Locus Names:	TV1239
ORF Names:	TVG1279046

Organism

Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1) [Complete proteome] [HAMAP]

Taxonomic identifier

273116 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma › Thermoplasma volcanium

Protein attributes

Sequence length	142 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme By similarity. HAMAP-Rule MF_02115
Catalytic activity	ATP + FMN = diphosphate + FAD. HAMAP-Rule MF_02115
Cofactor	Divalent metal cations By similarity.
Pathway	Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. HAMAP-Rule MF_02115
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the archaeal FAD synthase family.

Ontologies

Keywords
Ligand	ATP-binding FAD FMN Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	FAD biosynthetic process Inferred from electronic annotation. Source: HAMAP FMN metabolic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP FMN adenylyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 142

142

FAD synthase HAMAP-Rule MF_02115

PRO_0000406287

Regions

Nucleotide binding

9 – 10

2

ATP HAMAP-Rule MF_02115

Nucleotide binding

14 – 17

4

ATP HAMAP-Rule MF_02115

Nucleotide binding

91 – 94

4

ATP HAMAP-Rule MF_02115

Sites

Binding site

120

1

ATP; via amide nitrogen

Secondary structure

1

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142

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

15 – 25

11

Beta strand

28 – 35

8

Helix

38 – 43

6

Helix

52 – 59

8

Beta strand

66 – 70

5

Helix

76 – 83

8

Beta strand

86 – 90

5

Helix

95 – 108

14

Beta strand

113 – 116

4

Sequences

	Sequence		Length	Mass (Da)
	Q979C2 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: B9A106F982D0022E	FASTA	142	16,009
	10 20 30 40 50 60 MIRVMATGVF DILHLGHIHY LKESKKLGDE LVVVVARDST ARNNGKIPIF DENSRLALIS 70 80 90 100 110 120 ELKVVDRAIL GHEGDMMKTV IEVKPDIITL GYDQKFDEAE LQSKINKLGI TVKIVRISKY 130 140 DGQLNSSSSV RKKIMELIGE RY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium." Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y., Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T., Yamamoto Y., Aramaki H., Makino K., Suzuki M. Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1.
[2]	"The crystal structure of the lipopolysaccharide core biosynthesis protein from Thermoplasma volcanium GSS1." Midwest center for structural genomics (MCSG) Submitted (MAY-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH AMP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000011 Genomic DNA. Translation: BAB60381.1.

RefSeq

NP_111734.1. NC_002689.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GLV	X-ray	1.99	A/B	1-142	[»]

ProteinModelPortal

Q979C2.

ModBase

Search...

Protein-protein interaction databases

STRING

273116.TVN1215.

Protocols and materials databases

DNASU

1441355.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAB60381; BAB60381; BAB60381.

GeneID

1441355.

KEGG

tvo:TVN1215.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0615.

KO

K14656.

OMA

VAHDETV.

ProtClustDB

CLSK227867.

Enzyme and pathway databases

UniPathway

UPA00277; UER00407.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

HAMAP

MF_02115. FAD_synth_arch.

InterPro

IPR004821. Cyt_trans-like.
IPR024902. FAD_synth_RibL.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Pfam

PF01467. CTP_transf_2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00125. cyt_tran_rel. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q979C2.

Entry information

Entry name

RIBL_THEVO

Accession

Primary (citable) accession number: Q979C2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 5, 2011
Last sequence update:	October 1, 2001
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program