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B7K0C3 (B7K0C3_CYAP8) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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:PCC8801_3439 EMBL ACK67407.1
OrganismCyanothece sp. (strain PCC 8801) (Synechococcus sp. (strain PCC 8801 / RF-1)) [Complete proteome] [HAMAP] EMBL ACK67407.1
Taxonomic identifier41431 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece

Protein attributes

Sequence length556 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

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

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. SAAS SAAS016299 HAMAP-Rule MF_01283

Cofactor

Binds 1 zinc ion per subunit By similarity. SAAS SAAS016299 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. SAAS SAAS016299 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 binding264 – 2685GTP By similarity HAMAP-Rule MF_01283
Nucleotide binding307 – 3093GTP By similarity HAMAP-Rule MF_01283
Region1 – 211211DHBP synthase By similarity HAMAP-Rule MF_01283
Region35 – 362D-ribulose 5-phosphate binding By similarity HAMAP-Rule MF_01283
Region150 – 1545D-ribulose 5-phosphate binding By similarity HAMAP-Rule MF_01283
Region212 – 556345GTP cyclohydrolase II By similarity HAMAP-Rule MF_01283

Sites

Active site3411Proton acceptor; for GTP cyclohydrolase activity By similarity HAMAP-Rule MF_01283
Active site3431Nucleophile; for GTP cyclohydrolase activity By similarity HAMAP-Rule MF_01283
Metal binding361Magnesium or manganese 1 By similarity HAMAP-Rule MF_01283
Metal binding361Magnesium or manganese 2 By similarity HAMAP-Rule MF_01283
Metal binding1531Magnesium or manganese 2 By similarity HAMAP-Rule MF_01283
Metal binding2691Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2801Zinc; catalytic By similarity HAMAP-Rule MF_01283
Metal binding2821Zinc; catalytic By similarity HAMAP-Rule MF_01283
Binding site401D-ribulose 5-phosphate By similarity HAMAP-Rule MF_01283
Binding site1741D-ribulose 5-phosphate By similarity HAMAP-Rule MF_01283
Binding site2851GTP By similarity HAMAP-Rule MF_01283
Binding site3291GTP By similarity HAMAP-Rule MF_01283
Binding site3641GTP By similarity HAMAP-Rule MF_01283
Binding site3691GTP By similarity HAMAP-Rule MF_01283
Site1361Essential for DHBP synthase activity By similarity HAMAP-Rule MF_01283
Site1741Essential for DHBP synthase activity By similarity HAMAP-Rule MF_01283

Sequences

Sequence LengthMass (Da)Tools
B7K0C3 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: ABDD8DBF8EF3DE98

FASTA55661,992
        10         20         30         40         50         60 
MDASPNAIAQ FDTIDAALAD IKAGKAIIVV DDENRENEGD LICAAQFATP NMINFMAVEA 

        70         80         90        100        110        120 
RGLICLAMMG ERLDTLDLPL MVTKNTDSNQ TAFTVSIDAA KHLGVSTGIS AEDRARTIQV 

       130        140        150        160        170        180 
AINPDTHPDD LTRPGHIFPI RAKEGGVLKR AGHTEAAVDL SRLAGLYPAG VICEIQNPDG 

       190        200        210        220        230        240 
SMARLPELFE YAKKHELKLI SIADLISYRL KHDRFVYRET VCQFPSQFGT FQLYAYRNVL 

       250        260        270        280        290        300 
DGTEHVAIVK GDPAQFKDQP VMVRMHSECL TGDALGSMRC DCRMQLQTAL KMIEGSGLGV 

       310        320        330        340        350        360 
VVYLRQEGRG IGLVNKLKAY SLQDMGLDTV EANERLGFPA DLRDYGMGAQ MLNDLGVKQI 

       370        380        390        400        410        420 
RLITNNPRKI AGLKGYGLEV VDRVPLLIEA NDYNANYLAT KAEKLGHLLL HTYLITVAID 

       430        440        450        460        470        480 
WETEMRSAKE RYGNLEKLRQ LCRSSQLLLQ EEVRPIANAL FSSPSLIFHL GFEQGKMVDP 

       490        500        510        520        530        540 
HWYHNSKHPY LSAIAQILDE IVTWPNIKRL EFLISSGDDP LLGLQVQLDR HTFSLKDQPS 

       550 
EYLRELEMQT IYSFQG 

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References

[1]"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 8801.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001287 Genomic DNA. Translation: ACK67407.1.
RefSeqYP_002373563.1. NC_011726.1.

3D structure databases

ProteinModelPortalB7K0C3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING41431.PCC8801_3439.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK67407; ACK67407; PCC8801_3439.
GeneID7103129.
KEGGcyp:PCC8801_3439.
PATRIC21579233. VBICyaSp125535_3621.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0108.
HOGENOMHOG000115440.
KOK14652.
OMAGKGLICM.
OrthoDBEOG679TK8.

Enzyme and pathway databases

BioCycCSP41431:GHLK-3480-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]
SUPFAMSSF55821. SSF55821. 1 hit.
TIGRFAMsTIGR00505. ribA. 1 hit.
TIGR00506. ribB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB7K0C3_CYAP8
AccessionPrimary (citable) accession number: B7K0C3
Entry history
Integrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: June 11, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)