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P81453

- TGAS_STRMB

UniProt

P81453 - TGAS_STRMB

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Protein

Protein-glutamine gamma-glutamyltransferase

Gene
N/A
Organism
Streptomyces mobaraensis (Streptoverticillium mobaraense)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei140 – 1401
Active sitei331 – 3311
Active sitei350 – 3501

GO - Molecular functioni

  1. protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Propeptidei32 – 76451 PublicationPRO_0000033656Add
BLAST
Chaini77 – 407331Protein-glutamine gamma-glutamyltransferasePRO_0000033657Add
BLAST

Keywords - PTMi

Zymogen

Structurei

Secondary structure

1
407
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi42 – 465Combined sources
Helixi50 – 6112Combined sources
Beta strandi102 – 1065Combined sources
Helixi107 – 11610Combined sources
Turni117 – 1193Combined sources
Helixi130 – 1367Combined sources
Helixi142 – 1487Combined sources
Beta strandi156 – 1583Combined sources
Helixi163 – 17210Combined sources
Helixi181 – 19111Combined sources
Helixi195 – 21319Combined sources
Helixi219 – 23214Combined sources
Helixi236 – 2394Combined sources
Beta strandi242 – 2443Combined sources
Helixi245 – 2484Combined sources
Turni249 – 2524Combined sources
Helixi254 – 2574Combined sources
Turni259 – 2646Combined sources
Helixi266 – 2683Combined sources
Beta strandi269 – 27810Combined sources
Helixi288 – 2936Combined sources
Turni296 – 2994Combined sources
Turni303 – 3053Combined sources
Beta strandi321 – 3244Combined sources
Beta strandi331 – 3366Combined sources
Helixi343 – 3453Combined sources
Beta strandi347 – 3537Combined sources
Beta strandi359 – 3635Combined sources
Beta strandi365 – 3706Combined sources
Helixi371 – 3755Combined sources
Beta strandi382 – 39211Combined sources
Beta strandi404 – 4063Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IU4X-ray2.40A/B/C/D77-407[»]
3IU0X-ray1.90A32-407[»]
ProteinModelPortaliP81453.
SMRiP81453. Positions 77-407.
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
Entry Method Resolution (Å) Chain Positions PDBsum
1IU4 X-ray 2.40 A/B/C/D 77-407 [» ]
3IU0 X-ray 1.90 A 32-407 [» ]
ProteinModelPortali P81453.
SMRi P81453. Positions 77-407.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P81453.

Family and domain databases

Gene3Di 3.90.1360.10. 1 hit.
InterProi IPR015107. Transglut_prok.
[Graphical view ]
Pfami PF09017. Transglut_prok. 1 hit.
[Graphical view ]
PIRSFi PIRSF037210. Transglut_prok. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Secretion of active-form Streptoverticillium mobaraense transglutaminase by Corynebacterium glutamicum: processing of the pro-transglutaminase by a cosecreted subtilisin-like protease from Streptomyces albogriseolus."
    Kikuchi Y., Date M., Yokoyama K., Umezawa Y., Matsui H.
    Appl. Environ. Microbiol. 69:358-366(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 29032 / CBS 199.75 / DSM 40847 / NBRC 13819 / NCIMB 11159 / NRRL B-3729 / VKM Ac-928.
  2. "Confirmation of the genes coding a transglutaminase and a prolyl tri/tetrapeptidyl aminopeptidase from Streptomyces mobaraensis."
    Zindel S., Froels S., Kletzin A., Pfeifer F., Fuchsbauer H.L.
    Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 29032 / CBS 199.75 / DSM 40847 / NBRC 13819 / NCIMB 11159 / NRRL B-3729 / VKM Ac-928.
  3. "Bacterial pro-transglutaminase from Streptoverticillium mobaraense: purification, characterisation and sequence of the zymogen."
    Pasternack R., Dorsch S., Otterbach J.T., Robenek I.R., Wolf S., Fuchsbauer H.-L.
    Eur. J. Biochem. 257:570-576(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-407, PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 27441 / CBS 777.72 / DSM 40587 / JCM 4778 / NBRC 13476 / VKM Ac-879.
  4. "Primary structure of microbial transglutaminase from Streptoverticillium sp. strain s-8112."
    Kanaji T., Ozaki H., Takao T., Kawajiri H., Ide H., Motoki M., Shimonishi Y.
    J. Biol. Chem. 268:11565-11572(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 77-407, MASS SPECTROMETRY.
    Strain: S-8112.
  5. "Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense."
    Kashiwagi T., Yokoyama K., Ishikawa K., Ono K., Ejima D., Matsui H., Suzuki E.
    J. Biol. Chem. 277:44252-44260(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 77-407.
    Strain: ATCC 29032 / CBS 199.75 / DSM 40847 / NBRC 13819 / NCIMB 11159 / NRRL B-3729 / VKM Ac-928.

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 26, 2014
This is version 71 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

External Data

Dasty 3