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Protein

Riboflavin biosynthesis protein RibBA

Gene

ribBA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.UniRule 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 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

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 (ribBA)
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.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Riboflavin biosynthesis protein RibBA (ribBA)
  2. Riboflavin biosynthesis protein RibD (ribD)
  3. Riboflavin biosynthesis protein RibD (ribD)
  4. 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YitU (yitU), 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YwtE (ywtE), 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YcsE (ycsE)
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 bindingi27Magnesium or manganese 1UniRule annotation1
Metal bindingi27Magnesium or manganese 2UniRule annotation1
Binding sitei31D-ribulose 5-phosphateUniRule annotation1
Sitei124Essential for DHBP synthase activityUniRule annotation1
Metal bindingi141Magnesium or manganese 2UniRule annotation1
Binding sitei162D-ribulose 5-phosphateUniRule annotation1
Sitei162Essential for DHBP synthase activityUniRule annotation1
Metal bindingi256Zinc; catalyticUniRule annotation1
Metal bindingi267Zinc; catalyticUniRule annotation1
Metal bindingi269Zinc; catalyticUniRule annotation1
Binding sitei272GTPUniRule annotation1
Binding sitei316GTPUniRule annotation1
Active sitei328Proton acceptor; for GTP cyclohydrolase activityUniRule annotation1
Active sitei330Nucleophile; for GTP cyclohydrolase activityUniRule annotation1
Binding sitei351GTPUniRule annotation1
Binding sitei356GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi251 – 255GTPUniRule annotation5
Nucleotide bindingi294 – 296GTPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Lyase, Multifunctional enzyme
Biological processRiboflavin biosynthesis
LigandGTP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU23260-MONOMER
UniPathwayiUPA00275; UER00399
UPA00275; UER00400

Names & Taxonomyi

Protein namesi
Recommended name:
Riboflavin biosynthesis protein RibBAUniRule annotation
Including the following 2 domains:
3,4-dihydroxy-2-butanone 4-phosphate synthaseUniRule annotation (EC:4.1.99.12UniRule annotation)
Short name:
DHBP synthaseUniRule annotation
GTP cyclohydrolase-2UniRule annotation (EC:3.5.4.25UniRule annotation)
Alternative name(s):
GTP cyclohydrolase IIUniRule annotation
Gene namesi
Name:ribBAUniRule annotation
Synonyms:ribA
Ordered Locus Names:BSU23260
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001517211 – 398Riboflavin biosynthesis protein RibBAAdd BLAST398

Proteomic databases

PaxDbiP17620
PRIDEiP17620

Interactioni

Protein-protein interaction databases

IntActiP17620, 1 interactor
MINTiP17620
STRINGi224308.Bsubs1_010100012771

Structurei

3D structure databases

ProteinModelPortaliP17620
SMRiP17620
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 199DHBP synthaseAdd BLAST199
Regioni26 – 27D-ribulose 5-phosphate bindingUniRule annotation2
Regioni138 – 142D-ribulose 5-phosphate bindingUniRule annotation5
Regioni200 – 398GTP cyclohydrolase IIAdd BLAST199

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C66 Bacteria
COG0108 LUCA
COG0807 LUCA
HOGENOMiHOG000115440
InParanoidiP17620
KOiK14652
OMAiGCTTGIS
PhylomeDBiP17620

Family and domain databases

CDDicd00641 GTP_cyclohydro2, 1 hit
Gene3Di3.40.50.10990, 1 hit
HAMAPiMF_00179 RibA, 1 hit
MF_00180 RibB, 1 hit
MF_01283 RibBA, 1 hit
InterProiView protein in InterPro
IPR017945 DHBP_synth_RibB-like_a/b_dom
IPR000422 DHBP_synthase_RibB
IPR032677 GTP_cyclohydro_II
IPR000926 RibA
IPR036144 RibA-like_sf
IPR016299 Riboflavin_synth_RibBA
PfamiView protein in Pfam
PF00926 DHBP_synthase, 1 hit
PF00925 GTP_cyclohydro2, 1 hit
SUPFAMiSSF142695 SSF142695, 1 hit
SSF55821 SSF55821, 1 hit
TIGRFAMsiTIGR00505 ribA, 1 hit
TIGR00506 ribB, 1 hit

Sequencei

Sequence statusi: Complete.

P17620-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFHPIEEALD ALKKGEVIIV VDDEDRENEG DFVALAEHAT PEVINFMATH
60 70 80 90 100
GRGLICTPLS EEIADRLDLH PMVEHNTDSH HTAFTVSIDH RETKTGISAQ
110 120 130 140 150
ERSFTVQALL DSKSVPSDFQ RPGHIFPLIA KKGGVLKRAG HTEAAVDLAE
160 170 180 190 200
ACGSPGAGVI CEIMNEDGTM ARVPELIEIA KKHQLKMITI KDLIQYRYNL
210 220 230 240 250
TTLVEREVDI TLPTDFGTFK VYGYTNEVDG KEHVAFVMGD VPFGEEPVLV
260 270 280 290 300
RVHSECLTGD VFGSHRCDCG PQLHAALNQI AAEGRGVLLY LRQEGRGIGL
310 320 330 340 350
INKLKAYKLQ EQGYDTVEAN EALGFLPDLR NYGIGAQILR DLGVRNMKLL
360 370 380 390
TNNPRKIAGL EGYGLSISER VPLQMEAKEH NKKYLQTKMN KLGHLLHF
Length:398
Mass (Da):44,121
Last modified:August 1, 1990 - v1
Checksum:iD9162EA7DAE611AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09228 Genomic DNA Translation: AAA67483.1
X51510 Genomic DNA Translation: CAA35880.1
AL009126 Genomic DNA Translation: CAB14258.1
PIRiS45545
RefSeqiNP_390207.1, NC_000964.3
WP_004398484.1, NZ_JNCM01000036.1

Genome annotation databases

EnsemblBacteriaiCAB14258; CAB14258; BSU23260
GeneIDi938946
KEGGibsu:BSU23260
PATRICifig|224308.179.peg.2533

Similar proteinsi

Entry informationi

Entry nameiRIBBA_BACSU
AccessioniPrimary (citable) accession number: P17620
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: May 23, 2018
This is version 138 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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