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Protein

Glucan 1,4-alpha-maltotetraohydrolase

Gene

amyP

Organism
Pseudomonas stutzeri (Pseudomonas perfectomarina)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends.3 Publications

Cofactori

Ca2+3 PublicationsNote: Binds 2 calcium ions per subunit.3 Publications

Pathwayi: starch degradation

This protein is involved in the pathway starch degradation, which is part of Glycan degradation.2 Publications
View all proteins of this organism that are known to be involved in the pathway starch degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi22Calcium 13 Publications1
Metal bindingi23Calcium 1; via carbonyl oxygen3 Publications1
Metal bindingi34Calcium 13 Publications1
Metal bindingi37Calcium 13 Publications1
Metal bindingi38Calcium 13 Publications1
Metal bindingi137Calcium 23 Publications1
Binding sitei138Substrate2 Publications1
Metal bindingi172Calcium 23 Publications1
Metal bindingi175Calcium 2; via carbonyl oxygen3 Publications1
Metal bindingi183Calcium 23 Publications1
Binding sitei212Substrate2 Publications1
Active sitei214Nucleophile1 Publication1
Metal bindingi218Calcium 2; via carbonyl oxygen3 Publications1
Active sitei240Proton donor2 Publications1
Binding sitei314Substrate2 Publications1
Sitei315Transition state stabilizer1 Publication1
Binding sitei326Substrate1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00153.

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan 1,4-alpha-maltotetraohydrolase (EC:3.2.1.603 Publications)
Short name:
G4-amylase
Alternative name(s):
Exo-maltotetraohydrolase
Maltotetraose-forming amylase
Maltotetraose-forming exo-amylase
Gene namesi
Name:amyP
OrganismiPseudomonas stutzeri (Pseudomonas perfectomarina)
Taxonomic identifieri316 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi214D → N: Abolishes enzyme activity. 1 Publication1
Mutagenesisi240E → Q: Abolishes enzyme activity. 2 Publications1
Mutagenesisi315D → N: Abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Add BLAST21
ChainiPRO_000000142022 – 548Glucan 1,4-alpha-maltotetraohydrolaseAdd BLAST527

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi161 ↔ 1713 Publications
Disulfide bondi237 ↔ 2723 Publications

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1548
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi34 – 36Combined sources3
Beta strandi40 – 42Combined sources3
Helixi48 – 51Combined sources4
Turni53 – 55Combined sources3
Helixi56 – 69Combined sources14
Beta strandi73 – 77Combined sources5
Beta strandi87 – 89Combined sources3
Beta strandi92 – 94Combined sources3
Beta strandi102 – 104Combined sources3
Beta strandi108 – 110Combined sources3
Helixi113 – 125Combined sources13
Beta strandi129 – 134Combined sources6
Beta strandi152 – 155Combined sources4
Helixi158 – 160Combined sources3
Beta strandi165 – 167Combined sources3
Beta strandi172 – 174Combined sources3
Beta strandi180 – 184Combined sources5
Helixi189 – 205Combined sources17
Beta strandi208 – 214Combined sources7
Helixi216 – 218Combined sources3
Helixi221 – 231Combined sources11
Beta strandi235 – 239Combined sources5
Helixi245 – 247Combined sources3
Helixi253 – 256Combined sources4
Helixi259 – 270Combined sources12
Helixi277 – 285Combined sources9
Helixi288 – 293Combined sources6
Helixi295 – 297Combined sources3
Helixi301 – 304Combined sources4
Beta strandi307 – 309Combined sources3
Turni314 – 316Combined sources3
Helixi322 – 324Combined sources3
Helixi333 – 335Combined sources3
Helixi336 – 345Combined sources10
Beta strandi346 – 353Combined sources8
Helixi354 – 358Combined sources5
Helixi363 – 376Combined sources14
Beta strandi383 – 386Combined sources4
Beta strandi390 – 398Combined sources9
Beta strandi403 – 409Combined sources7
Helixi415 – 417Combined sources3
Beta strandi424 – 429Combined sources6
Turni430 – 433Combined sources4
Beta strandi434 – 438Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GCYX-ray1.60A22-548[»]
1JDAX-ray2.20A22-450[»]
1JDCX-ray1.90A22-450[»]
1JDDX-ray1.90A22-450[»]
1QI3X-ray2.00A22-450[»]
1QI4X-ray2.00A22-439[»]
1QI5X-ray2.00A22-439[»]
1QPKX-ray2.00A22-439[»]
2AMGX-ray2.00A22-439[»]
ProteinModelPortaliP13507.
SMRiP13507.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13507.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini446 – 548CBM20PROSITE-ProRule annotationAdd BLAST103

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni99 – 100Substrate binding1 Publication2
Regioni177 – 181Substrate binding1 Publication5
Regioni217 – 218Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated
Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015165. DUF1921.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF00686. CBM_20. 1 hit.
PF09081. DUF1921. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P13507-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHILRAAVL AAMLLPLPSM ADQAGKSPNA VRYHGGDEII LQGFHWNVVR
60 70 80 90 100
EAPNDWYNIL RQQAATIAAD GFSAIWMPVP WRDFSSWSDG SKSGGGEGYF
110 120 130 140 150
WHDFNKNGRY GSDAQLRQAA SALGGAGVKV LYDVVPNHMN RGYPDKEINL
160 170 180 190 200
PAGQGFWRND CADPGNYPND CDDGDRFIGG DADLNTGHPQ VYGMFRDEFT
210 220 230 240 250
NLRSQYGAGG FRFDFVRGYA PERVNSWMTD SADNSFCVGE LWKGPSEYPN
260 270 280 290 300
WDWRNTASWQ QIIKDWSDRA KCPVFDFALK ERMQNGSIAD WKHGLNGNPD
310 320 330 340 350
PRWREVAVTF VDNHDTGYSP GQNGGQHHWA LQDGLIRQAY AYILTSPGTP
360 370 380 390 400
VVYWSHMYDW GYGDFIRQLI QVRRAAGVRA DSAISFHSGY SGLVATVSGS
410 420 430 440 450
QQTLVVALNS DLGNPGQVAS GSFSEAVNAS NGQVRVWRSG TGSGGGEPGA
460 470 480 490 500
LVSVSFRCDN GATQMGDSVY AVGNVSQLGN WSPAAALRLT DTSGYPTWKG
510 520 530 540
SIALPAGQNE EWKCLIRNEA NATQVRQWQG GANNSLTPSE GATTVGRL
Length:548
Mass (Da):59,876
Last modified:November 1, 1997 - v2
Checksum:i2B87217B3379158F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti286 – 302GSIAD…NPDPR → ARSPTGSTPERQSRPA AA sequence (PubMed:2646279).CuratedAdd BLAST17

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24516 Genomic DNA. Translation: AAA25707.1.
PIRiA32803.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24516 Genomic DNA. Translation: AAA25707.1.
PIRiA32803.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GCYX-ray1.60A22-548[»]
1JDAX-ray2.20A22-450[»]
1JDCX-ray1.90A22-450[»]
1JDDX-ray1.90A22-450[»]
1QI3X-ray2.00A22-450[»]
1QI4X-ray2.00A22-439[»]
1QI5X-ray2.00A22-439[»]
1QPKX-ray2.00A22-439[»]
2AMGX-ray2.00A22-439[»]
ProteinModelPortaliP13507.
SMRiP13507.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00153.

Miscellaneous databases

EvolutionaryTraceiP13507.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015165. DUF1921.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF00686. CBM_20. 1 hit.
PF09081. DUF1921. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMT4_PSEST
AccessioniPrimary (citable) accession number: P13507
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There are several isoenzyme forms of this protein.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.