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Protein

Protein-glutamine gamma-glutamyltransferase

Gene
N/A
Organism
Streptomyces mobaraensis (Streptoverticillium mobaraense)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.

Catalytic activityi

Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1401
Active sitei3311
Active sitei3501

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.2.13. 6129.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-glutamine gamma-glutamyltransferase (EC:2.3.2.13)
Alternative name(s):
MTG
Transglutaminase
Short name:
TGase
OrganismiStreptomyces mobaraensis (Streptoverticillium mobaraense)
Taxonomic identifieri35621 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Pathology & Biotechi

Biotechnological usei

Sold under the name Activa TG by Ajinomoto. It has the ability to cross-link protein molecules present in food without the use of salt or binders. Used to improve some of the physical properties such as firmness, elasticity and moisture retention of food such as meat, poultry and seafood.

Protein family/group databases

Allergomei11851. Str mo TG.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
PropeptideiPRO_000003365632 – 761 PublicationAdd BLAST45
ChainiPRO_000003365777 – 407Protein-glutamine gamma-glutamyltransferaseAdd BLAST331

Keywords - PTMi

Zymogen

Structurei

Secondary structure

1407
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi42 – 46Combined sources5
Helixi50 – 61Combined sources12
Beta strandi102 – 106Combined sources5
Helixi107 – 116Combined sources10
Turni117 – 119Combined sources3
Helixi130 – 136Combined sources7
Helixi142 – 148Combined sources7
Beta strandi156 – 158Combined sources3
Helixi163 – 172Combined sources10
Helixi181 – 191Combined sources11
Helixi195 – 213Combined sources19
Helixi219 – 232Combined sources14
Helixi236 – 239Combined sources4
Beta strandi242 – 244Combined sources3
Helixi245 – 248Combined sources4
Turni249 – 252Combined sources4
Helixi254 – 257Combined sources4
Turni259 – 264Combined sources6
Helixi266 – 268Combined sources3
Beta strandi269 – 278Combined sources10
Helixi288 – 293Combined sources6
Turni296 – 299Combined sources4
Turni303 – 305Combined sources3
Beta strandi321 – 324Combined sources4
Beta strandi331 – 336Combined sources6
Helixi343 – 345Combined sources3
Beta strandi347 – 353Combined sources7
Beta strandi359 – 363Combined sources5
Beta strandi365 – 370Combined sources6
Helixi371 – 375Combined sources5
Beta strandi382 – 392Combined sources11
Beta strandi404 – 406Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IU4X-ray2.40A/B/C/D77-407[»]
3IU0X-ray1.90A32-407[»]
ProteinModelPortaliP81453.
SMRiP81453.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81453.

Family & Domainsi

Sequence similaritiesi

Belongs to the bacterial TGase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.90.1360.10. 1 hit.
InterProiIPR015107. Transglut_prok.
[Graphical view]
PfamiPF09017. Transglut_prok. 1 hit.
[Graphical view]
PIRSFiPIRSF037210. Transglut_prok. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P81453-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIRRRALVF ATMSAVLCTA GFMPSAGEAA ADNGAGEETK SYAETYRLTA
60 70 80 90 100
DDVANINALN ESAPAASSAG PSFRAPDSDD RVTPPAEPLD RMPDPYRPSY
110 120 130 140 150
GRAETVVNNY IRKWQQVYSH RDGRKQQMTE EQREWLSYGC VGVTWVNSGQ
160 170 180 190 200
YPTNRLAFAS FDEDRFKNEL KNGRPRSGET RAEFEGRVAK ESFDEEKGFQ
210 220 230 240 250
RAREVASVMN RALENAHDES AYLDNLKKEL ANGNDALRNE DARSPFYSAL
260 270 280 290 300
RNTPSFKERN GGNHDPSRMK AVIYSKHFWS GQDRSSSADK RKYGDPDAFR
310 320 330 340 350
PAPGTGLVDM SRDRNIPRSP TSPGEGFVNF DYGWFGAQTE ADADKTVWTH
360 370 380 390 400
GNHYHAPNGS LGAMHVYESK FRNWSEGYSD FDRGAYVITF IPKSWNTAPD

KVKQGWP
Length:407
Mass (Da):45,684
Last modified:November 7, 2003 - v2
Checksum:i10F7F7A04EAB2DF4
GO

Mass spectrometryi

Molecular mass is 37869.2±8.8 Da from positions 77 - 407. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF531437 Genomic DNA. Translation: AAM95951.1.
HF968462 Genomic DNA. Translation: CCW72544.1.
Y18315 Genomic DNA. Translation: CAA77128.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF531437 Genomic DNA. Translation: AAM95951.1.
HF968462 Genomic DNA. Translation: CCW72544.1.
Y18315 Genomic DNA. Translation: CAA77128.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IU4X-ray2.40A/B/C/D77-407[»]
3IU0X-ray1.90A32-407[»]
ProteinModelPortaliP81453.
SMRiP81453.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei11851. Str mo TG.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.3.2.13. 6129.

Miscellaneous databases

EvolutionaryTraceiP81453.

Family and domain databases

Gene3Di3.90.1360.10. 1 hit.
InterProiIPR015107. Transglut_prok.
[Graphical view]
PfamiPF09017. Transglut_prok. 1 hit.
[Graphical view]
PIRSFiPIRSF037210. Transglut_prok. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTGAS_STRMB
AccessioniPrimary (citable) accession number: P81453
Secondary accession number(s): N1NTU7, Q8KRJ2, Q9ZAF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 7, 2003
Last modified: November 2, 2016
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.