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Q6MCT5

- Q6MCT5_PARUW

UniProt

Q6MCT5 - Q6MCT5_PARUW

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Protein

Riboflavin biosynthesis protein RibBA

Gene
ribA, ribBA, pc0890
Organism
Protochlamydia amoebophila (strain UWE25)
Status
Unreviewed - 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 By similarity.UniRule annotationSAAS annotations
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate By similarity.UniRule annotationSAAS annotations

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 annotations

Cofactori

Binds 1 zinc ion per subunit By similarity.UniRule annotationSAAS annotations
Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity.UniRule annotation

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi253 – 2575GTP By similarityUniRule annotation
Nucleotide bindingi297 – 2993GTP By similarityUniRule annotation

GO - Molecular functioni

  1. 3,4-dihydroxy-2-butanone-4-phosphate synthase activity Source: UniProtKB-HAMAP
  2. GTP binding Source: UniProtKB-KW
  3. GTP cyclohydrolase II activity Source: UniProtKB-HAMAP
  4. magnesium ion binding Source: UniProtKB-HAMAP
  5. manganese ion binding Source: UniProtKB-HAMAP
  6. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. riboflavin biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotationImported, LyaseUniRule annotation

Keywords - Biological processi

Riboflavin biosynthesisUniRule annotationSAAS annotations

Keywords - Ligandi

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

Enzyme and pathway databases

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

Names & Taxonomyi

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

Interactioni

Protein-protein interaction databases

STRINGi264201.pc0890.

Structurei

3D structure databases

ProteinModelPortaliQ6MCT5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 202202DHBP synthase By similarityUniRule annotationAdd
BLAST
Regioni27 – 282D-ribulose 5-phosphate binding By similarityUniRule annotation
Regioni141 – 1455D-ribulose 5-phosphate binding By similarityUniRule annotation
Regioni203 – 412210GTP cyclohydrolase II By similarityUniRule 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.
OMAiGKGLICM.
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

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MKTYRLEDAL LALKEGKFVI VVDDENRENE GDLILAAEKA HPSSLGFMIR    50
HTTGIICLAM KGQRLDELKL PPMVTDNTDR KQTAFTVSVD YLHQGVTTGV 100
SAEDRTKTIL SLIHPHTKPE DLGRPGHIFP LRYKEGGVLK RAGHTEAAVD 150
LTNLAKLYPA GILAELINED GSMMRLPELE KFSDLHQIPI ITIAELIRFR 200
RRHEKLVSCF SQSPIPTPFG DFNAYVYESQ LDGIQHIALV KGEIKNQKNI 250
LVRMHSECLT GDVFGSKRCD CGSQLKLAME KIEQEGRGVI IYLRGHEGRG 300
IGIGHKLKAY NLQDQGKDTL EANLELGFPI DSREYGIGAQ ILVDLGLSTI 350
RLMTNNLAKY NGLAGYDLEI TERVPLPVCV TKENKHYLQT KKDKLGHLID 400
LSEDKLEIHH ST 412
Length:412
Mass (Da):46,075
Last modified:July 5, 2004 - v1
Checksum:i5D48E399C35CF8B0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX908798 Genomic DNA. Translation: CAF23614.1.
RefSeqiYP_007889.1. NC_005861.1.

Genome annotation databases

EnsemblBacteriaiCAF23614; CAF23614; pc0890.
GeneIDi2780041.
KEGGipcu:pc0890.
PATRICi31997129. VBICanPro72727_0904.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX908798 Genomic DNA. Translation: CAF23614.1 .
RefSeqi YP_007889.1. NC_005861.1.

3D structure databases

ProteinModelPortali Q6MCT5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 264201.pc0890.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAF23614 ; CAF23614 ; pc0890 .
GeneIDi 2780041.
KEGGi pcu:pc0890.
PATRICi 31997129. VBICanPro72727_0904.

Phylogenomic databases

eggNOGi COG0108.
HOGENOMi HOG000115440.
KOi K14652.
OMAi GKGLICM.
OrthoDBi EOG679TK8.

Enzyme and pathway databases

UniPathwayi UPA00275 ; UER00399 .
UPA00275 ; UER00400 .
BioCyci PAMO264201:GH0M-914-MONOMER.

Family and domain databases

Gene3Di 3.90.870.10. 1 hit.
HAMAPi MF_00179. RibA.
MF_00180. RibB.
MF_01283. RibBA.
InterProi IPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR000926. GTP_CycHdrlaseII_RibA.
IPR016299. Riboflavin_synth_RibBA.
[Graphical view ]
Pfami PF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view ]
PIRSFi PIRSF001259. RibA. 1 hit.
SUPFAMi SSF55821. SSF55821. 1 hit.
TIGRFAMsi TIGR00505. ribA. 1 hit.
TIGR00506. ribB. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UWE25.

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 11, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzymeUniRule annotation

External Data

Dasty 3

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