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P13507

- AMT4_PSEST

UniProt

P13507 - AMT4_PSEST

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Protein

Glucan 1,4-alpha-maltotetraohydrolase

Gene

amyP

Organism
Pseudomonas stutzeri (Pseudomonas perfectomarina)
Status
Reviewed - 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.

Cofactori

Binds 2 calcium ions per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi22 – 221Calcium 1
Metal bindingi23 – 231Calcium 1; via carbonyl oxygen
Metal bindingi34 – 341Calcium 1
Metal bindingi37 – 371Calcium 1
Metal bindingi38 – 381Calcium 1
Metal bindingi137 – 1371Calcium 2
Binding sitei138 – 1381Substrate
Metal bindingi172 – 1721Calcium 2
Metal bindingi175 – 1751Calcium 2; via carbonyl oxygen
Metal bindingi183 – 1831Calcium 2
Binding sitei212 – 2121Substrate
Active sitei214 – 2141Nucleophile1 Publication
Metal bindingi218 – 2181Calcium 2; via carbonyl oxygen
Active sitei240 – 2401Proton donor1 Publication
Binding sitei314 – 3141Substrate
Sitei315 – 3151Transition state stabilizerBy similarity
Binding sitei326 – 3261Substrate

GO - Molecular functioni

  1. glucan 1,4-alpha-maltotetraohydrolase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. starch binding Source: InterPro

GO - Biological processi

  1. starch catabolic process Source: UniProtKB-UniPathway
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:3.2.1.60)
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

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 548527Glucan 1,4-alpha-maltotetraohydrolasePRO_0000001420Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi161 ↔ 1711 Publication
Disulfide bondi237 ↔ 2721 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
548
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 363
Beta strandi40 – 423
Helixi48 – 514
Turni53 – 553
Helixi56 – 6914
Beta strandi73 – 775
Beta strandi87 – 893
Beta strandi92 – 943
Beta strandi102 – 1043
Beta strandi108 – 1103
Helixi113 – 12513
Beta strandi129 – 1346
Beta strandi152 – 1554
Helixi158 – 1603
Beta strandi165 – 1673
Beta strandi172 – 1743
Beta strandi180 – 1845
Helixi189 – 20517
Beta strandi208 – 2147
Helixi216 – 2183
Helixi221 – 23111
Beta strandi235 – 2395
Helixi245 – 2473
Helixi253 – 2564
Helixi259 – 27012
Helixi277 – 2859
Helixi288 – 2936
Helixi295 – 2973
Helixi301 – 3044
Beta strandi307 – 3093
Turni314 – 3163
Helixi322 – 3243
Helixi333 – 3353
Helixi336 – 34510
Beta strandi346 – 3538
Helixi354 – 3585
Helixi363 – 37614
Beta strandi383 – 3864
Beta strandi390 – 3989
Beta strandi403 – 4097
Helixi415 – 4173
Beta strandi424 – 4296
Turni430 – 4334
Beta strandi434 – 4385

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 22-439.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13507.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini446 – 548103CBM20PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1002Substrate bindingBy similarity
Regioni177 – 1815Substrate binding

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.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
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.
SMARTiSM01065. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti286 – 30217GSIAD…NPDPR → ARSPTGSTPERQSRPA AA sequence (PubMed:2646279)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M24516 Genomic DNA. Translation: AAA25707.1.
PIRiA32803.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M24516 Genomic DNA. Translation: AAA25707.1 .
PIRi A32803.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GCY X-ray 1.60 A 22-548 [» ]
1JDA X-ray 2.20 A 22-450 [» ]
1JDC X-ray 1.90 A 22-450 [» ]
1JDD X-ray 1.90 A 22-450 [» ]
1QI3 X-ray 2.00 A 22-450 [» ]
1QI4 X-ray 2.00 A 22-439 [» ]
1QI5 X-ray 2.00 A 22-439 [» ]
1QPK X-ray 2.00 A 22-439 [» ]
2AMG X-ray 2.00 A 22-439 [» ]
ProteinModelPortali P13507.
SMRi P13507. Positions 22-439.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM20. Carbohydrate-Binding Module Family 20.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00153 .

Miscellaneous databases

EvolutionaryTracei P13507.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015165. DUF1921.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF00686. CBM_20. 1 hit.
PF09081. DUF1921. 1 hit.
[Graphical view ]
PRINTSi PR00110. ALPHAAMYLASE.
SMARTi SM01065. CBM_2. 1 hit.
[Graphical view ]
SUPFAMi SSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEi PS51166. CBM20. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and nucleotide sequence of the gene (amyP) for maltotetraose-forming amylase from Pseudomonas stutzeri MO-19."
    Fujita M., Torigoe K., Nakada T., Tsusaki K., Kubota M., Sakai S., Tsujisaka Y.
    J. Bacteriol. 171:1333-1339(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: MO-19.
  2. "Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri."
    Morishita Y., Hasegawa K., Matsuura Y., Katsube Y., Kubota M., Sakai S.
    J. Mol. Biol. 267:661-672(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SEQUENCE REVISION TO 286-302.
    Strain: MO-19.
  3. "Crystal structures of a mutant maltotetraose-forming exo-amylase cocrystallized with maltopentaose."
    Yoshioka Y., Hasegawa K., Matsuura Y., Katsube Y., Kubota M.
    J. Mol. Biol. 271:619-628(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT GLN-240 IN COMPLEX WITH MALTOPENTAOSE, CALCIUM IONS.
    Strain: MO-19.
  4. "Roles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase."
    Hasegawa K., Kubota M., Matsuura Y.
    Protein Eng. 12:819-824(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF VARIANTS IN COMPLEXES WITH CALCIUM IONS AND MALTOTETRAOSE, DISULFIDE BONDS, ACTIVE SITE.
    Strain: MO-19.

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: October 29, 2014
This is version 112 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

External Data

Dasty 3