Q9PES5 (Q9PES5_XYLFA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
GTP cyclohydrolase II/3,4-dihydroxy-2-butanone 4-phosphate synthase EMBL AAF83763.1

Gene names

Ordered Locus Names:

XF_0953

Organism

Xylella fastidiosa [Complete proteome] [HAMAP]

Taxonomic identifier

2371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Protein existence	Inferred 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. SAAS SAAS000422
Catalytic activity	D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. SAAS SAAS000422
Cofactor	Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity. SAAS SAAS000422
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. SAAS SAAS000422

Ontologies

Keywords
Biological process	Riboflavin biosynthesis SAAS SAAS000422
Ligand	Magnesium SAAS SAAS000422 Manganese SAAS SAAS000422 Metal-binding SAAS SAAS000422
Molecular function	Hydrolase EMBL AAF83763.1 Lyase SAAS SAAS000422
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3,4-dihydroxy-2-butanone-4-phosphate synthase activity Inferred from electronic annotation. Source: InterPro GTP cyclohydrolase II activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9PES5 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B5ECE9BC194CCA41	FASTA	377	41,057
	10 20 30 40 50 60 MNSFAAVPVL IEEIRAGRMV VIVDDEDREN EGDLIMAAEL VAPKDINFMV THARGLVCLS 70 80 90 100 110 120 LTRERCAQIG LSPMVQRNTT RFQTNFTVSI EAAEGLTTGI SAYDRAHTIR TAVRPNAKPS 130 140 150 160 170 180 DLHQPGHIFP LIAQPGGVLT RAGHTEAAND LPMLAGLEPA GVLVEIMNAD GTMARRPQLE 190 200 210 220 230 240 VFAQQHGLKI GSIADLIAYR LANEHTVERV DERVIETEYG SFLLVTYRDR IAHDLHFALV 250 260 270 280 290 300 RGTLDASIPT LVRVQVENPL ADMLHWRRED FGVAASDALR MIAAAERGVM VVLAAPRDSD 310 320 330 340 350 360 ALLARLRREP EVVSNVKDVG QWRRNGAGGQ ILADLGLGKL RVLGTPRRQI ALAGFGLEVL 370 EYVECRGGAP VAPQGVD

References

[1]

"The genome sequence of the plant pathogen Xylella fastidiosa." Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M., Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S., Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S., Bueno M.R.P., Camargo A.A., Camargo L.E.A. , Carraro D.M., Carrer H., Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M., Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H., Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C. Nature 406:151-159(2000) [PubMed: 10910347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9a5c.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003849 Genomic DNA. Translation: AAF83763.1.
PIR	B82741.
RefSeq	NP_298243.1. NC_002488.3.
3D structure databases
HSSP	HSSP built from PDB template 1G58 based on UniProtKB P24199.
ProteinModelPortal	Q9PES5.
SMR	Q9PES5. Positions 4-204.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1126489.
GenomeReviews	Gene locus XF_0953 in contig AE003849_GR.
KEGG	xfa:XF0953.
NMPDR	fig|160492.1.peg.950.
PATRIC	24131960. VBIXylFas578_1019.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG735778.
OMA	IEYRSRT.
ProtClustDB	CLSK446132.
Enzyme and pathway databases
BioCyc	XFAS160492:XF0953-MONOMER.
Family and domain databases
HAMAP	MF_00180. RibB. [Tree]
InterPro	IPR017945. DHBP_synth_RibB-like_a/b_dom. IPR000422. DHBP_synthase_RibB. IPR000926. GTP_CycHdrlaseII_RibA. IPR016299. Riboflavin_synth_RibBA. [Graphical view]
Gene3D	G3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
KO	K14652.
Pfam	PF00926. DHBP_synthase. 1 hit. PF00925. GTP_cyclohydro2. 1 hit. [Graphical view]
PIRSF	PIRSF001259. RibA. 1 hit.
SUPFAM	SSF55821. DHBP_synth_RibB-like_a/b_dom. 1 hit.
TIGRFAMs	TIGR00506. RibB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

Q9PES5_XYLFA

Accession

Primary (citable) accession number: Q9PES5

Entry history

Integrated into UniProtKB/TrEMBL:	October 1, 2000
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)