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Protein

Multifunctional fusion protein

Gene

deoC

Organism
uncultured bacterium Contig1532b
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.UniRule annotation
Phosphotransfer between the C1 and C5 carbon atoms of pentose.UniRule annotationSAAS annotation

Catalytic activityi

2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde.UniRule annotation
2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-alpha-D-ribose 5-phosphate.UniRule annotationSAAS annotation
Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate.UniRule annotationSAAS annotation

Cofactori

Mn2+UniRule annotationNote: Binds 1 or 2 manganese ions.UniRule annotation

Pathwayi: 2-deoxy-D-ribose 1-phosphate degradation

This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Multifunctional fusion protein (deoC)
This subpathway is part of the pathway 2-deoxy-D-ribose 1-phosphate degradation, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate, the pathway 2-deoxy-D-ribose 1-phosphate degradation and in Carbohydrate degradation.

Pathwayi: 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II).UniRule annotationSAAS annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Multifunctional fusion protein (deoC)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi11ManganeseUniRule annotation1
Metal bindingi299ManganeseUniRule annotation1
Metal bindingi335ManganeseUniRule annotation1
Metal bindingi336ManganeseUniRule annotation1
Metal bindingi347ManganeseUniRule annotation1
Active sitei491Proton donor/acceptorUniRule annotation1
Active sitei555Schiff-base intermediate with acetaldehydeUniRule annotation1
Active sitei584Proton donor/acceptorUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomeraseUniRule annotationSAAS annotation, LyaseUniRule annotation
LigandManganeseUniRule annotationSAAS annotation, Metal-bindingUniRule annotationSAAS annotation, Schiff baseUniRule annotation

Enzyme and pathway databases

UniPathwayi
UPA00002;UER00468

UPA00087;UER00173

Names & Taxonomyi

Protein namesi
Recommended name:
Multifunctional fusion proteinUniRule annotation
Including the following 2 domains:
Deoxyribose-phosphate aldolaseUniRule annotation (EC:4.1.2.4UniRule annotation)
Short name:
DERAUniRule annotation
Alternative name(s):
2-deoxy-D-ribose 5-phosphate aldolaseUniRule annotation
PhosphodeoxyriboaldolaseUniRule annotation
Short name:
DeoxyriboaldolaseUniRule annotation
PhosphopentomutaseUniRule annotation (EC:5.4.2.7UniRule annotation)
Alternative name(s):
PhosphodeoxyribomutaseUniRule annotation
Gene namesi
Name:deoCUniRule annotation
Synonyms:deoBUniRule annotation
Organismiuncultured bacterium Contig1532bImported
Taxonomic identifieri1393450 [NCBI]
Taxonomic lineageiBacteriaenvironmental samples

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 381MetalloenzymeInterPro annotationAdd BLAST379

Sequence similaritiesi

Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily.UniRule annotation
Belongs to the phosphopentomutase family.UniRule annotationSAAS annotation

Family and domain databases

CDDicd00959 DeoC, 1 hit
cd16009 PPM, 1 hit
Gene3Di3.20.20.70, 1 hit
3.30.70.1250, 1 hit
3.40.720.10, 1 hit
HAMAPiMF_00114 DeoC_type1, 1 hit
MF_00740 Phosphopentomut, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR017849 Alkaline_Pase-like_a/b/a
IPR017850 Alkaline_phosphatase_core_sf
IPR010045 DeoB
IPR011343 DeoC
IPR002915 DeoC/FbaB/lacD_aldolase
IPR028581 DeoC_typeI
IPR006124 Metalloenzyme
IPR024052 Phosphopentomutase_DeoB_cap_sf
PANTHERiPTHR21110 PTHR21110, 1 hit
PfamiView protein in Pfam
PF01791 DeoC, 1 hit
PF01676 Metalloenzyme, 1 hit
SMARTiView protein in SMART
SM01133 DeoC, 1 hit
SUPFAMiSSF143856 SSF143856, 1 hit
SSF53649 SSF53649, 1 hit
TIGRFAMsiTIGR01696 deoB, 1 hit
TIGR00126 deoC, 1 hit

Sequencei

Sequence statusi: Complete.

W0FLJ6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKRVFLIIL DSLGCGNAPD ASAFGDQGSN TLAAVLSASD KPFPNLSSMG
60 70 80 90 100
LFDIDGNSDP RILEYLSKDP QAGRPAPIGA YGRLREESSG GKDSTIGHWE
110 120 130 140 150
IAGVVSEDPQ PTYPDGFPSY VVDKLKEISG RGVLCNLPYS GTQAIEDYGE
160 170 180 190 200
EHFSSGDLIL YTSADSVLQI AAHEEIVPLD ELYRICREMR TFMTGKDAVG
210 220 230 240 250
RIIARPFTGT PGSFTRTANR HDFAVEAPSA TMMDHLKAKG FDVISVGKIY
260 270 280 290 300
DLFAGRGFTE TNPTKGNSEG IAKIREYLDK DFTGLLFSNL VDFDMLYGHR
310 320 330 340 350
NNIEGYNEAL HEFDDALGDI LESLKEDDLL IISADHGCDP STVSTDHSRE
360 370 380 390 400
QVPLLIYGKG YSTPRNLGSI TGFSYISQVV VNALSGARFE KRFPERDLDP
410 420 430 440 450
SDPGDVMTYV DLTNLKVTAT EDDIKALIDR AIASKTMSVC IPPCYVRSAY
460 470 480 490 500
DYARGRIPIC TVIGFPNGYN TTSVKVTEAK DAVDNGACEI DMVINVAFVK
510 520 530 540 550
AGKMKEVEDE VKAIAGAVHE KGAILKVIIE ACLLTEEEKV ALCGIVERCG
560 570 580 590 600
AEYIKTSTGF STGGATVEDV ALMRANLSSS VRIKAAGGIR SPEAARAMID
610
AGATRIGASG L
Length:611
Mass (Da):65,770
Last modified:March 19, 2014 - v1
Checksum:i49872CD062DC4B71
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KC246771 Genomic DNA Translation: AHF23687.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KC246771 Genomic DNA Translation: AHF23687.1

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00002;UER00468

UPA00087;UER00173

Family and domain databases

CDDicd00959 DeoC, 1 hit
cd16009 PPM, 1 hit
Gene3Di3.20.20.70, 1 hit
3.30.70.1250, 1 hit
3.40.720.10, 1 hit
HAMAPiMF_00114 DeoC_type1, 1 hit
MF_00740 Phosphopentomut, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR017849 Alkaline_Pase-like_a/b/a
IPR017850 Alkaline_phosphatase_core_sf
IPR010045 DeoB
IPR011343 DeoC
IPR002915 DeoC/FbaB/lacD_aldolase
IPR028581 DeoC_typeI
IPR006124 Metalloenzyme
IPR024052 Phosphopentomutase_DeoB_cap_sf
PANTHERiPTHR21110 PTHR21110, 1 hit
PfamiView protein in Pfam
PF01791 DeoC, 1 hit
PF01676 Metalloenzyme, 1 hit
SMARTiView protein in SMART
SM01133 DeoC, 1 hit
SUPFAMiSSF143856 SSF143856, 1 hit
SSF53649 SSF53649, 1 hit
TIGRFAMsiTIGR01696 deoB, 1 hit
TIGR00126 deoC, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiW0FLJ6_9BACT
AccessioniPrimary (citable) accession number: W0FLJ6
Entry historyiIntegrated into UniProtKB/TrEMBL: March 19, 2014
Last sequence update: March 19, 2014
Last modified: November 7, 2018
This is version 34 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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