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D2RNY5 (D2RNY5_ACIFV) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Riboflavin biosynthesis protein RibBA HAMAP-Rule MF_01283
Gene names
Name:ribBA HAMAP-Rule MF_01283
Ordered Locus Names:Acfer_0355 EMBL ADB46761.1
OrganismAcidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4) [Complete proteome] [HAMAP] EMBL ADB46761.1
Taxonomic identifier591001 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Negativicutes › Selenomonadales › Acidaminococcaceae › Acidaminococcus ›

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate By similarity. HAMAP-Rule MF_01283 SAAS SAAS000422

Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate By similarity. HAMAP-Rule MF_01283 SAAS SAAS000422

Catalytic activity

D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. HAMAP-Rule MF_01283

GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate. HAMAP-Rule MF_01283

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01283

Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity. HAMAP-Rule MF_01283

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP-Rule MF_01283

Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4. HAMAP-Rule MF_01283

Sequence similarities

In the C-terminal section; belongs to the GTP cyclohydrolase II family. HAMAP-Rule MF_01283

In the N-terminal section; belongs to the DHBP synthase family. HAMAP-Rule MF_01283

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding255 – 2595GTP By similarity HAMAP-Rule MF_01283
Nucleotide binding298 – 3003GTP By similarity HAMAP-Rule MF_01283
Region1 – 204204DHBP synthase By similarity HAMAP-Rule MF_01283
Region31 – 322D-ribulose 5-phosphate binding By similarity HAMAP-Rule MF_01283
Region143 – 1475D-ribulose 5-phosphate binding By similarity HAMAP-Rule MF_01283
Region205 – 408204GTP cyclohydrolase II By similarity HAMAP-Rule MF_01283

Sites

Active site3321Proton acceptor; for GTP cyclohydrolase activity By similarity HAMAP-Rule MF_01283
Active site3341Nucleophile; for GTP cyclohydrolase activity By similarity HAMAP-Rule MF_01283
Metal binding321Magnesium or manganese 1 By similarity HAMAP-Rule MF_01283
Metal binding321Magnesium or manganese 2 By similarity HAMAP-Rule MF_01283
Metal binding1461Magnesium or manganese 2 By similarity HAMAP-Rule MF_01283
Metal binding2601Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2711Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2731Zinc; catalytic By similarity HAMAP-Rule MF_01283
Binding site361D-ribulose 5-phosphate By similarity HAMAP-Rule MF_01283
Binding site1671D-ribulose 5-phosphate By similarity HAMAP-Rule MF_01283
Binding site2761GTP By similarity HAMAP-Rule MF_01283
Binding site3201GTP By similarity HAMAP-Rule MF_01283
Binding site3551GTP By similarity HAMAP-Rule MF_01283
Binding site3601GTP By similarity HAMAP-Rule MF_01283
Site1291Essential for DHBP synthase activity By similarity HAMAP-Rule MF_01283
Site1671Essential for DHBP synthase activity By similarity HAMAP-Rule MF_01283

Sequences

Sequence LengthMass (Da)Tools
D2RNY5 [UniParc].

Last modified March 2, 2010. Version 1.
Checksum: E9C03148F8FE9109

FASTA40845,199
        10         20         30         40         50         60 
MDKKFQFAPI EQAIEDIRAG KMVLVTDDPD RENEGDLIMS AEYVTPDDIN FMATHAKGLI 

        70         80         90        100        110        120 
CMPCDGAILD RLQMEPMVAN NTDNHETAFT VSIDHKDTTT GISAVERAYT IKKCTDESAK 

       130        140        150        160        170        180 
PEDFRRPGHV FPLRSREGGV LRRTGHTETT TDLCRLAGLK PVGICCEIMS ADGTMARTPE 

       190        200        210        220        230        240 
LIEFARKFNL TFITVADLIA YRKKNEKMVH RIANVALPSK YGTFRAIGYE NDLDDKCHVA 

       250        260        270        280        290        300 
IIKGDVAGKK DVLVRVHSEC LTGDALGSLR CDCGDQLATS LKMIEKEGCG VVLYMQQEGR 

       310        320        330        340        350        360 
GIGLANKLRA YELQDQGLDT VDANVKLGFK PDMRDYGIGA QILADLGLTS IRLMTNNPAK 

       370        380        390        400 
RAGLSGYGIT ITETVPIIMK DNCYNHRYMV TKQVRMGHEL HEDVEDAK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001859 Genomic DNA. Translation: ADB46761.1.
RefSeqYP_003398076.1. NC_013740.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADB46761; ADB46761; Acfer_0355.
GeneID8736803.
KEGGafn:Acfer_0355.
PATRIC31907259. VBIAciFer109666_0376.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000115440.
KOK14652.
OMALMVDRNT.

Enzyme and pathway databases

BioCycAFER591001:GHUL-373-MONOMER.
UniPathwayUPA00275; UER00399.
UPA00275; UER00400.

Family and domain databases

Gene3D3.90.870.10. 1 hit.
HAMAPMF_00179. RibA.
MF_00180. RibB.
MF_01283. RibBA.
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR000926. GTP_CycHdrlaseII_RibA.
IPR016299. Riboflavin_synth_RibBA.
[Graphical view]
PfamPF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
PIRSFPIRSF001259. RibA. 1 hit.
SUPFAMSSF55821. SSF55821. 1 hit.
TIGRFAMsTIGR00505. ribA. 1 hit.
TIGR00506. ribB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD2RNY5_ACIFV
AccessionPrimary (citable) accession number: D2RNY5
Entry history
Integrated into UniProtKB/TrEMBL: March 2, 2010
Last sequence update: March 2, 2010
Last modified: February 19, 2014
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info