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MYCTU:OTSA

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Species (Taxon ID) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332)
Gene Name(s) otsA
Protein Name(s) Trehalose-phosphate synthase

TPS Trehalose-6-phosphate synthase

External Links
UniProt P9WN11
EMBL AL123456
PIR G70569
RefSeq NP_218007.1
YP_006516979.1
ProteinModelPortal P9WN11
SMR P9WN11
GeneID 13317097
888404
KEGG mtu:Rv3490
mtv:RVBD_3490
TubercuList Rv3490
KO K00697
OMA VVGFHIP
PhylomeDB P9WN11
Reactome REACT_27232
UniPathway UPA00299
Proteomes UP000001584
GO GO:0005618
GO:0005886
GO:0047260
GO:0003825
GO:0030145
GO:0040007
GO:0005992
InterPro IPR001830
Pfam PF00982

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0005992

trehalose biosynthetic process

PMID:12473104[1]

ECO:0000314

P

Fig.4 synthesis of trehalose using UDP-Glc and GDP-Glc correlates with amount or enzyme and has a linear relationship with time Fig.5 increased trehalose-P synthesized correlates with increase amount of TPS protein.

complete
CACAO 4398

involved_in

GO:0005992

trehalose biosynthetic process

PMID:12473104[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:14532352[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005618

cell wall

PMID:20825248[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005618

cell wall

PMID:15525680[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0047260

alpha,alpha-trehalose-phosphate synthase (GDP-forming) activity

PMID:12473104[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0030145

manganese ion binding

PMID:12473104[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0005992

trehalose biosynthetic process

PMID:10658666[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003825

alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity

PMID:10658666[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0070415

trehalose metabolism in response to cold stress

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11751
PANTHER:PTN001646917

P

Seeded From UniProt

complete

involved_in

GO:0070413

trehalose metabolism in response to stress

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000082159
PomBase:SPAC328.03
SGD:S000002481

P

Seeded From UniProt

complete

enables

GO:0047260

alpha,alpha-trehalose-phosphate synthase (GDP-forming) activity

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001646917
UniProtKB:P9WN11

F

Seeded From UniProt

complete

enables

GO:0030145

manganese ion binding

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001646917
UniProtKB:P9WN11

F

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11751
PANTHER:PTN001646917

P

Seeded From UniProt

complete

involved_in

GO:0006970

response to osmotic stress

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11751
PANTHER:PTN001646917

P

Seeded From UniProt

complete

involved_in

GO:0005992

trehalose biosynthetic process

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11751
FB:FBgn0027560
PANTHER:PTN000082159
SGD:S000000330
SGD:S000002481
SGD:S000004566
SGD:S000004874
TAIR:locus:2200216
UniProtKB:O59921
UniProtKB:P9WN11
UniProtKB:Q4WHW0
UniProtKB:Q4WLM9
WB:WBGene00001649

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11751
PANTHER:PTN000082159
TAIR:locus:2054027
TAIR:locus:2202290

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000082159
TAIR:locus:2202990
WB:WBGene00001649

C

Seeded From UniProt

complete

contributes_to

GO:0004805

trehalose-phosphatase activity

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0027560
PANTHER:PTN000082159
PomBase:SPAC19G12.15c
SGD:S000000330
SGD:S000002481
SGD:S000004566
SGD:S000004874
UniProtKB:Q5AI14
WB:WBGene00001649

F

Seeded From UniProt

complete

contributes_to

GO:0003825

alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000182821
PANTHER:PTN000082159
PomBase:SPAC328.03
SGD:S000000330
SGD:S000004566
SGD:S000004874
TAIR:locus:2202990

F

Seeded From UniProt

complete

involved_in

GO:0016311

dephosphorylation

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004805

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001830

F

Seeded From UniProt

complete

involved_in

GO:0005992

trehalose biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001830

P

Seeded From UniProt

complete

enables

GO:0003825

alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.4.1.15

F

Seeded From UniProt

complete

involved_in

GO:0005992

trehalose biosynthetic process

Reactome:R-MTU-868688

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

Reactome:R-MTU-868622

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0016757

transferase activity, transferring glycosyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0328

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

involved_in

GO:0005992

trehalose biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00299

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 Pan, YT et al. (2002) Trehalose-phosphate synthase of Mycobacterium tuberculosis. Cloning, expression and properties of the recombinant enzyme. Eur. J. Biochem. 269 6091-100 PubMed GONUTS page
  2. Gu, S et al. (2003) Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Mol. Cell Proteomics 2 1284-96 PubMed GONUTS page
  3. Wolfe, LM et al. (2010) Proteomic definition of the cell wall of Mycobacterium tuberculosis. J. Proteome Res. 9 5816-26 PubMed GONUTS page
  4. Mawuenyega, KG et al. (2005) Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Mol. Biol. Cell 16 396-404 PubMed GONUTS page
  5. 5.0 5.1 De Smet, KA et al. (2000) Three pathways for trehalose biosynthesis in mycobacteria. Microbiology (Reading, Engl.) 146 ( Pt 1) 199-208 PubMed GONUTS page
  6. 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page