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Protein

Riboflavin biosynthesis protein RibBA

Gene

ribBA

Organism
Cyanothece sp. (strain PCC 8801) (Synechococcus sp. (strain PCC 8801 / RF-1))
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 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 (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.SAAS 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 (PCC8801_1230)
  3. Riboflavin biosynthesis protein RibD (PCC8801_1230)
  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 bindingi36Magnesium or manganese 1UniRule annotation1
Metal bindingi36Magnesium or manganese 2UniRule annotation1
Binding sitei40D-ribulose 5-phosphateUniRule annotation1
Sitei136Essential for DHBP synthase activityUniRule annotation1
Metal bindingi153Magnesium or manganese 2UniRule annotation1
Binding sitei174D-ribulose 5-phosphateUniRule annotation1
Sitei174Essential for DHBP synthase activityUniRule annotation1
Metal bindingi269Zinc; catalyticUniRule annotation1
Metal bindingi280Zinc; catalyticUniRule annotation1
Metal bindingi282Zinc; catalyticUniRule annotation1
Binding sitei285GTPUniRule annotation1
Binding sitei329GTPUniRule annotation1
Active sitei341Proton acceptor; for GTP cyclohydrolase activityUniRule annotation1
Active sitei343Nucleophile; for GTP cyclohydrolase activityUniRule annotation1
Binding sitei364GTPUniRule annotation1
Binding sitei369GTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi264 – 268GTPUniRule annotation5
Nucleotide bindingi307 – 309GTPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolaseUniRule annotationImported, LyaseUniRule annotationSAAS annotation
Biological processRiboflavin biosynthesisUniRule annotationSAAS annotation
LigandGTP-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 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
Ordered Locus Names:PCC8801_3439Imported
OrganismiCyanothece sp. (strain PCC 8801) (Synechococcus sp. (strain PCC 8801 / RF-1))Imported
Taxonomic identifieri41431 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesCyanothecaceaeCyanothece
Proteomesi
  • UP000008204 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi41431.PCC8801_3439.

Structurei

3D structure databases

ProteinModelPortaliB7K0C3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini221 – 385GTP_cyclohydro2InterPro annotationAdd BLAST165

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 211DHBP synthaseUniRule annotationAdd BLAST211
Regioni35 – 36D-ribulose 5-phosphate bindingUniRule annotation2
Regioni150 – 154D-ribulose 5-phosphate bindingUniRule annotation5
Regioni212 – 556GTP cyclohydrolase IIUniRule annotationAdd BLAST345

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.
OMAiGCTTGIS.
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.
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.

B7K0C3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDASPNAIAQ FDTIDAALAD IKAGKAIIVV DDENRENEGD LICAAQFATP
60 70 80 90 100
NMINFMAVEA RGLICLAMMG ERLDTLDLPL MVTKNTDSNQ TAFTVSIDAA
110 120 130 140 150
KHLGVSTGIS AEDRARTIQV AINPDTHPDD LTRPGHIFPI RAKEGGVLKR
160 170 180 190 200
AGHTEAAVDL SRLAGLYPAG VICEIQNPDG SMARLPELFE YAKKHELKLI
210 220 230 240 250
SIADLISYRL KHDRFVYRET VCQFPSQFGT FQLYAYRNVL DGTEHVAIVK
260 270 280 290 300
GDPAQFKDQP VMVRMHSECL TGDALGSMRC DCRMQLQTAL KMIEGSGLGV
310 320 330 340 350
VVYLRQEGRG IGLVNKLKAY SLQDMGLDTV EANERLGFPA DLRDYGMGAQ
360 370 380 390 400
MLNDLGVKQI RLITNNPRKI AGLKGYGLEV VDRVPLLIEA NDYNANYLAT
410 420 430 440 450
KAEKLGHLLL HTYLITVAID WETEMRSAKE RYGNLEKLRQ LCRSSQLLLQ
460 470 480 490 500
EEVRPIANAL FSSPSLIFHL GFEQGKMVDP HWYHNSKHPY LSAIAQILDE
510 520 530 540 550
IVTWPNIKRL EFLISSGDDP LLGLQVQLDR HTFSLKDQPS EYLRELEMQT

IYSFQG
Length:556
Mass (Da):61,992
Last modified:February 10, 2009 - v1
Checksum:iABDD8DBF8EF3DE98
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001287 Genomic DNA. Translation: ACK67407.1.
RefSeqiWP_012596667.1. NC_011726.1.

Genome annotation databases

EnsemblBacteriaiACK67407; ACK67407; PCC8801_3439.
KEGGicyp:PCC8801_3439.

Similar proteinsi

Entry informationi

Entry nameiB7K0C3_CYAP8
AccessioniPrimary (citable) accession number: B7K0C3
Entry historyiIntegrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: November 22, 2017
This is version 75 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzymeUniRule annotation, Reference proteomeImported