Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8Q095

- RIBL_METMA

UniProt

Q8Q095 - RIBL_METMA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

FAD synthase

Gene

ribL

Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme.UniRule annotation

Catalytic activityi

ATP + FMN = diphosphate + FAD.UniRule annotation

Cofactori

Divalent metal cations.UniRule annotation

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi21 – 222ATPUniRule annotation
Nucleotide bindingi26 – 294ATPUniRule annotation
Nucleotide bindingi102 – 1054ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. FMN adenylyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. FAD biosynthetic process Source: UniProtKB-HAMAP
  2. FMN metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, FAD, Flavoprotein, FMN, Nucleotide-binding

Enzyme and pathway databases

BioCyciMMAZ192952:GCK2-255-MONOMER.
UniPathwayiUPA00277; UER00407.

Names & Taxonomyi

Protein namesi
Recommended name:
FAD synthaseUniRule annotation (EC:2.7.7.2UniRule annotation)
Alternative name(s):
FMN adenylyltransferaseUniRule annotation
Flavin adenine dinucleotide synthaseUniRule annotation
Gene namesi
Name:ribLUniRule annotation
Ordered Locus Names:MM_0242
OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Taxonomic identifieri192952 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
ProteomesiUP000000595: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 151151FAD synthasePRO_0000406270Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi192952.MM_0242.

Structurei

3D structure databases

ProteinModelPortaliQ8Q095.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the archaeal FAD synthase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0615.
HOGENOMiHOG000284153.
KOiK14656.
OMAiIVLGHDQ.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_02115. FAD_synth_arch.
InterProiIPR004821. Cyt_trans-like.
IPR024902. FAD_synth_RibL.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8Q095-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLAGYYPSPG DLLTRVLATG TFDILHPGHV YFLAQAKALG DELFVIIARD
60 70 80 90 100
SNVTHKPKPV IPEEQRLEMV DALKAVNKAI LGSEKDMFEP LREIKPDIIA
110 120 130 140 150
LGYDQRFDTE ILEKELTKRG LPAKVVRIPL SKECPLCSTG TIIKEVLKRY

G
Length:151
Mass (Da):16,859
Last modified:October 1, 2002 - v1
Checksum:i86106AACFE872651
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE008384 Genomic DNA. Translation: AAM29938.1.
RefSeqiNP_632266.1. NC_003901.1.
WP_011032196.1. NC_003901.1.

Genome annotation databases

EnsemblBacteriaiAAM29938; AAM29938; MM_0242.
GeneIDi1478584.
KEGGimma:MM_0242.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE008384 Genomic DNA. Translation: AAM29938.1 .
RefSeqi NP_632266.1. NC_003901.1.
WP_011032196.1. NC_003901.1.

3D structure databases

ProteinModelPortali Q8Q095.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 192952.MM_0242.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM29938 ; AAM29938 ; MM_0242 .
GeneIDi 1478584.
KEGGi mma:MM_0242.

Phylogenomic databases

eggNOGi COG0615.
HOGENOMi HOG000284153.
KOi K14656.
OMAi IVLGHDQ.

Enzyme and pathway databases

UniPathwayi UPA00277 ; UER00407 .
BioCyci MMAZ192952:GCK2-255-MONOMER.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_02115. FAD_synth_arch.
InterProi IPR004821. Cyt_trans-like.
IPR024902. FAD_synth_RibL.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
Pfami PF01467. CTP_transf_2. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00125. cyt_tran_rel. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
    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.
    J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Entry informationi

Entry nameiRIBL_METMA
AccessioniPrimary (citable) accession number: Q8Q095
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 66 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3