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Protein

Riboflavin biosynthesis protein RibBA

Gene

ribA

Organism
Protochlamydia amoebophila (strain UWE25)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.UniRule annotationSAAS annotation
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.UniRule annotationSAAS annotation

Catalytic activityi

D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate.UniRule annotation
GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.UniRule annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation, Mn2+UniRule annotationNote: Binds 2 divalent metal cations per subunit. Magnesium or manganese.UniRule annotation
  • Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathway: riboflavin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Riboflavin biosynthesis protein RibBA (ribA)
This subpathway is part of the pathway riboflavin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate, the pathway riboflavin biosynthesis and in Cofactor biosynthesis.

Pathway: riboflavin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-amino-6-(D-ribitylamino)uracil from GTP.UniRule annotationSAAS annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Riboflavin biosynthesis protein RibBA (ribA)
  2. Riboflavin biosynthesis protein RibD (ribD)
  3. Riboflavin biosynthesis protein RibD (ribD)
  4. no protein annotated in this organism
This subpathway is part of the pathway riboflavin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-6-(D-ribitylamino)uracil from GTP, the pathway riboflavin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi28 – 281Magnesium or manganese 1UniRule annotation
Metal bindingi28 – 281Magnesium or manganese 2UniRule annotation
Binding sitei32 – 321D-ribulose 5-phosphateUniRule annotation
Sitei127 – 1271Essential for DHBP synthase activityUniRule annotation
Metal bindingi144 – 1441Magnesium or manganese 2UniRule annotation
Binding sitei165 – 1651D-ribulose 5-phosphateUniRule annotation
Sitei165 – 1651Essential for DHBP synthase activityUniRule annotation
Metal bindingi258 – 2581Zinc; catalyticUniRule annotation
Metal bindingi269 – 2691Zinc; catalyticUniRule annotation
Metal bindingi271 – 2711Zinc; catalyticUniRule annotation
Binding sitei274 – 2741GTPUniRule annotation
Binding sitei319 – 3191GTPUniRule annotation
Active sitei331 – 3311Proton acceptor; for GTP cyclohydrolase activityUniRule annotation
Active sitei333 – 3331Nucleophile; for GTP cyclohydrolase activityUniRule annotation
Binding sitei354 – 3541GTPUniRule annotation
Binding sitei359 – 3591GTPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi253 – 2575GTPUniRule annotation
Nucleotide bindingi297 – 2993GTPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotation, LyaseUniRule annotationSAAS annotation

Keywords - Biological processi

Riboflavin biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

GTP-bindingUniRule annotationSAAS annotation, MagnesiumUniRule annotation, ManganeseUniRule annotation, Metal-bindingUniRule annotationSAAS annotation, Nucleotide-binding, ZincUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciPAMO264201:GH0M-914-MONOMER.
UniPathwayiUPA00275; UER00399.
UPA00275; UER00400.

Names & Taxonomyi

Protein namesi
Recommended name:
Riboflavin biosynthesis protein RibBAUniRule annotationSAAS annotation
Gene namesi
Name:ribAImported
Synonyms:ribBAUniRule annotation
Ordered Locus Names:pc0890Imported
OrganismiProtochlamydia amoebophila (strain UWE25)Imported
Taxonomic identifieri264201 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesParachlamydiaceaeCandidatus Protochlamydia
ProteomesiUP000000529 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi264201.pc0890.

Structurei

3D structure databases

ProteinModelPortaliQ6MCT5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 202202DHBP synthaseUniRule annotationAdd
BLAST
Regioni27 – 282D-ribulose 5-phosphate bindingUniRule annotation
Regioni141 – 1455D-ribulose 5-phosphate bindingUniRule annotation
Regioni203 – 412210GTP cyclohydrolase IIUniRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the GTP cyclohydrolase II family.UniRule annotation
In the N-terminal section; belongs to the DHBP synthase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0108.
HOGENOMiHOG000115440.
KOiK14652.
OMAiLMVDRNT.
OrthoDBiEOG679TK8.

Family and domain databases

Gene3Di3.90.870.10. 1 hit.
HAMAPiMF_00179. RibA.
MF_00180. RibB.
MF_01283. RibBA.
InterProiIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR000926. GTP_CycHdrlaseII_RibA.
IPR016299. Riboflavin_synth_RibBA.
[Graphical view]
PfamiPF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
PIRSFiPIRSF001259. RibA. 1 hit.
SUPFAMiSSF55821. SSF55821. 1 hit.
TIGRFAMsiTIGR00505. ribA. 1 hit.
TIGR00506. ribB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6MCT5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTYRLEDAL LALKEGKFVI VVDDENRENE GDLILAAEKA HPSSLGFMIR
60 70 80 90 100
HTTGIICLAM KGQRLDELKL PPMVTDNTDR KQTAFTVSVD YLHQGVTTGV
110 120 130 140 150
SAEDRTKTIL SLIHPHTKPE DLGRPGHIFP LRYKEGGVLK RAGHTEAAVD
160 170 180 190 200
LTNLAKLYPA GILAELINED GSMMRLPELE KFSDLHQIPI ITIAELIRFR
210 220 230 240 250
RRHEKLVSCF SQSPIPTPFG DFNAYVYESQ LDGIQHIALV KGEIKNQKNI
260 270 280 290 300
LVRMHSECLT GDVFGSKRCD CGSQLKLAME KIEQEGRGVI IYLRGHEGRG
310 320 330 340 350
IGIGHKLKAY NLQDQGKDTL EANLELGFPI DSREYGIGAQ ILVDLGLSTI
360 370 380 390 400
RLMTNNLAKY NGLAGYDLEI TERVPLPVCV TKENKHYLQT KKDKLGHLID
410
LSEDKLEIHH ST
Length:412
Mass (Da):46,075
Last modified:July 5, 2004 - v1
Checksum:i5D48E399C35CF8B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX908798 Genomic DNA. Translation: CAF23614.1.
RefSeqiWP_011175440.1. NC_005861.1.
YP_007889.1. NC_005861.1.

Genome annotation databases

EnsemblBacteriaiCAF23614; CAF23614; pc0890.
KEGGipcu:pc0890.
PATRICi31997129. VBICanPro72727_0904.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX908798 Genomic DNA. Translation: CAF23614.1.
RefSeqiWP_011175440.1. NC_005861.1.
YP_007889.1. NC_005861.1.

3D structure databases

ProteinModelPortaliQ6MCT5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi264201.pc0890.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAF23614; CAF23614; pc0890.
KEGGipcu:pc0890.
PATRICi31997129. VBICanPro72727_0904.

Phylogenomic databases

eggNOGiCOG0108.
HOGENOMiHOG000115440.
KOiK14652.
OMAiLMVDRNT.
OrthoDBiEOG679TK8.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00399.
UPA00275; UER00400.
BioCyciPAMO264201:GH0M-914-MONOMER.

Family and domain databases

Gene3Di3.90.870.10. 1 hit.
HAMAPiMF_00179. RibA.
MF_00180. RibB.
MF_01283. RibBA.
InterProiIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR000926. GTP_CycHdrlaseII_RibA.
IPR016299. Riboflavin_synth_RibBA.
[Graphical view]
PfamiPF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
PIRSFiPIRSF001259. RibA. 1 hit.
SUPFAMiSSF55821. SSF55821. 1 hit.
TIGRFAMsiTIGR00505. ribA. 1 hit.
TIGR00506. ribB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UWE25Imported.

Entry informationi

Entry nameiQ6MCT5_PARUW
AccessioniPrimary (citable) accession number: Q6MCT5
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 24, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzymeUniRule annotation, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.