Riboflavin biosynthesis protein ribBA

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Reviewed, UniProtKB/Swiss-Prot Q9PLJ5 (RIBBA_CHLMU)

Last modified November 3, 2009. Version 59. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Riboflavin biosynthesis protein ribBA
Including the following 2 domains:
    1- Recommended name:
            3,4-dihydroxy-2-butanone 4-phosphate synthase
                Short name=DHBP synthase
              EC=4.1.99.12
    2- Recommended name:
            GTP cyclohydrolase-2
              EC=3.5.4.25
        Alternative name(s):
            GTP cyclohydrolase II

Gene names

Name:	ribBA
Synonyms:	ribA/B
Ordered Locus Names:	TC_0104

Organism

Chlamydia muridarum [Complete proteome] [HAMAP]

Taxonomic identifier

83560 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia

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Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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General annotation (Comments)

Function	Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate By similarity. Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate By similarity.
Catalytic activity	D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. HAMAP MF_01283 GTP + 3 H₂O = formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate. HAMAP MF_01283
Cofactor	Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity. Binds 1 zinc ion per subunit By similarity.
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP MF_01283 Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4. HAMAP MF_01283
Sequence similarities	In the N-terminal section; belongs to the DHBP synthase family. In the C-terminal section; belongs to the GTP cyclohydrolase II family.

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Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Ligand	GTP-binding Magnesium Manganese Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase Lyase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	3,4-dihydroxy-2-butanone-4-phosphate synthase activity Inferred from electronic annotation. Source: HAMAP GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP cyclohydrolase II activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP manganese ion binding Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 424

424

Riboflavin biosynthesis protein ribBA HAMAP MF_01283

PRO_0000151723

Regions

Nucleotide binding

257 – 261

GTP By similarity

Nucleotide binding

301 – 303

GTP By similarity

Region

1 – 206

206

DHBP synthase HAMAP MF_01283

Region

32 – 33

D-ribulose 5-phosphate binding By similarity

Region

145 – 149

D-ribulose 5-phosphate binding By similarity

Region

207 – 424

218

GTP cyclohydrolase II HAMAP MF_01283

Sites

Active site

335

Proton acceptor; for GTP cyclohydrolase activity Potential

Active site

337

Nucleophile; for GTP cyclohydrolase activity By similarity

Metal binding

Magnesium or manganese 1 By similarity

Metal binding

Magnesium or manganese 2 By similarity

Metal binding

148

Magnesium or manganese 2 By similarity

Metal binding

262

Zinc; catalytic By similarity

Metal binding

273

Zinc; catalytic By similarity

Metal binding

275

Zinc; catalytic By similarity

Binding site

D-ribulose 5-phosphate By similarity

Binding site

169

D-ribulose 5-phosphate By similarity

Binding site

278

GTP By similarity

Binding site

323

GTP By similarity

Binding site

358

GTP By similarity

Binding site

363

GTP By similarity

Site

131

Essential for DHBP synthase activity By similarity

Site

169

Essential for DHBP synthase activity By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9PLJ5-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 0298128162BAC016
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FASTA

424

47,067

        10         20         30         40         50         60 
MVTCEAGIAS VQQAIKDIAD GNFVIVIDRE SRENEGDLIL AGEKVSAEKM AFLLSHTTGI 

        70         80         90        100        110        120 
VCASVTREQA RVLDLPAMVQ ENQCAFKTAF TVSVDASSGI TTGVSAADRT RTVQLLSDPT 

       130        140        150        160        170        180 
SISQSFVRPG HVFPLVSQPG GVVKRPGHTE ASMDLMRLAG MYPCGIFAEL VNADHSMMRQ 

       190        200        210        220        230        240 
QQILDFAEQH GFTVITVDDL ITYRWTFDSL VEHVSSARIP TKYGEFFIHV YKSIIDGTEH 

       250        260        270        280        290        300 
FALVKGDIRE QESVPVRVHS ECLTGDVLGS CRCDCGAQLD MAMRYIAEQG LGVIVYLRGQ 

       310        320        330        340        350        360 
EGRGIGFGHK IQAYALQDLG YDTVEANLQL SFPIDAREYG VAAQILKDLR LTSVRLITHN 

       370        380        390        400        410        420 
PKKFFELQRL GIHILDRIVL PVIVSSENER YLRTKKDRMG HWLNFPVLNE SEDEYETVER 


TSCC

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References

[1]

"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L.

Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MoPn / Nigg.

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Cross-references

Sequence databases
	AE002160 Genomic DNA. Translation: AAF38984.1.
PIR	B81740.
RefSeq	NP_296488.1.
3D structure databases
HSSP	HSSP built from PDB template 1G58 based on UniProtKB P24199.
ModBase	Search...
Genome annotation databases
GeneID	1245634.
GenomeReviews	Gene locus TC_0104 in contig AE002160_GR.
KEGG	cmu:TC0104.
TIGR	TC_0104.
Phylogenomic databases
HOGENOM	Q9PLJ5.
OMA	LRCDCRM.
Enzyme and pathway databases
BioCyc	CMUR243161:TC_0104-MON.
BRENDA	3.5.4.25. 256349. 4.1.99.12. 256349.
Family and domain databases
HAMAP	MF_01283. [Tree]
InterPro	IPR017945. DHBP_synth_RibB-like_a/b_dom. IPR000422. DHBP_synthase_RibB. IPR000926. GTP_CycHdrlase_II. IPR016299. Riboflavin_synth_RibA. [Graphical view]
Gene3D	G3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
Pfam	PF00926. DHBP_synthase. 1 hit. PF00925. GTP_cyclohydro2. 1 hit. [Graphical view]
PIRSF	PIRSF001259. RibA. 1 hit.
ProDom	PD003034. DHBP_synthase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00505. ribA. 1 hit. TIGR00506. ribB. 1 hit.
ProtoNet	Search...

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Entry information

Entry name

RIBBA_CHLMU

Accession

Primary (citable) accession number: Q9PLJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents