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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 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

Mg2+UniRule annotation, Mn2+UniRule annotationNote: Binds 2 divalent metal cations per subunit. Magnesium or manganese.UniRule annotation

Pathwayi: 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.

Pathwayi: riboflavin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-amino-6-(D-ribitylamino)uracil from GTP.SAAS 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)DescriptionActionsGraphical viewLength
Metal bindingi28Magnesium or manganese 1UniRule annotation1
Metal bindingi28Magnesium or manganese 2UniRule annotation1
Binding sitei32D-ribulose 5-phosphateUniRule annotation1
Sitei127Essential for DHBP synthase activityUniRule annotation1
Metal bindingi144Magnesium or manganese 2UniRule annotation1
Binding sitei165D-ribulose 5-phosphateUniRule annotation1
Sitei165Essential for DHBP synthase activityUniRule annotation1
Metal bindingi258Zinc; catalyticUniRule annotation1
Metal bindingi269Zinc; catalyticUniRule annotation1
Metal bindingi271Zinc; catalyticUniRule annotation1
Binding sitei274GTPUniRule annotation1
Binding sitei319GTPUniRule annotation1
Active sitei331Proton acceptor; for GTP cyclohydrolase activityUniRule annotation1
Active sitei333Nucleophile; for GTP cyclohydrolase activityUniRule annotation1
Binding sitei354GTPUniRule annotation1
Binding sitei359GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi253 – 257GTPUniRule annotation5
Nucleotide bindingi297 – 299GTPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotationImported, 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

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
Proteomesi
  • UP000000529 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi264201.pc0890.

Structurei

3D structure databases

ProteinModelPortaliQ6MCT5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini212 – 375GTP_cyclohydro2InterPro annotationAdd BLAST164

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 202DHBP synthaseUniRule annotationAdd BLAST202
Regioni27 – 28D-ribulose 5-phosphate bindingUniRule annotation2
Regioni141 – 145D-ribulose 5-phosphate bindingUniRule annotation5
Regioni203 – 412GTP cyclohydrolase IIUniRule annotationAdd BLAST210

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C66. Bacteria.
COG0108. LUCA.
COG0807. LUCA.
HOGENOMiHOG000115440.
KOiK14652.
OMAiLMVDRNT.
OrthoDBiPOG091H008U.

Family and domain databases

CDDicd00641. GTP_cyclohydro2. 1 hit.
Gene3Di3.90.870.10. 1 hit.
HAMAPiMF_00179. RibA. 1 hit.
MF_00180. RibB. 1 hit.
MF_01283. RibBA. 1 hit.
InterProiIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR032677. GTP_cyclohydro_II.
IPR000926. RibA.
IPR016299. Riboflavin_synth_RibBA.
[Graphical view]
PfamiPF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
SUPFAMiSSF142695. SSF142695. 1 hit.
SSF55821. 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.

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.

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

eggNOGiENOG4105C66. Bacteria.
COG0108. LUCA.
COG0807. LUCA.
HOGENOMiHOG000115440.
KOiK14652.
OMAiLMVDRNT.
OrthoDBiPOG091H008U.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00399.
UPA00275; UER00400.

Family and domain databases

CDDicd00641. GTP_cyclohydro2. 1 hit.
Gene3Di3.90.870.10. 1 hit.
HAMAPiMF_00179. RibA. 1 hit.
MF_00180. RibB. 1 hit.
MF_01283. RibBA. 1 hit.
InterProiIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR032677. GTP_cyclohydro_II.
IPR000926. RibA.
IPR016299. Riboflavin_synth_RibBA.
[Graphical view]
PfamiPF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
SUPFAMiSSF142695. SSF142695. 1 hit.
SSF55821. SSF55821. 1 hit.
TIGRFAMsiTIGR00505. ribA. 1 hit.
TIGR00506. ribB. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 94 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

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 one 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.