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Protein

Isoamylase

Gene

iam

Organism
Pseudomonas amyloderamosa
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins.1 Publication

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi154CalciumCombined sources1 Publication1
Metal bindingi255CalciumCombined sources1 Publication1
Metal bindingi256Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi258CalciumCombined sources1 Publication1
Metal bindingi285CalciumCombined sources1 Publication1
Active sitei401Nucleophile1
Active sitei461Proton donor1
Sitei536Transition state stabilizerBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.68. 5091.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Isoamylase (EC:3.2.1.681 Publication)
Gene namesi
Name:iam
OrganismiPseudomonas amyloderamosa
Taxonomic identifieri32043 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Add BLAST26
ChainiPRO_000000142427 – 776IsoamylaseAdd BLAST750

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi410 ↔ 422Combined sources1 Publication
Disulfide bondi546 ↔ 616Combined sources1 Publication
Disulfide bondi738 ↔ 766Combined sources1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP10342.

Expressioni

Inductioni

By maltose.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1776
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 37Combined sources4
Beta strandi41 – 49Combined sources9
Beta strandi54 – 66Combined sources13
Beta strandi70 – 74Combined sources5
Beta strandi82 – 88Combined sources7
Helixi89 – 94Combined sources6
Beta strandi102 – 109Combined sources8
Helixi163 – 166Combined sources4
Turni170 – 174Combined sources5
Turni178 – 180Combined sources3
Helixi202 – 204Combined sources3
Beta strandi207 – 210Combined sources4
Helixi212 – 216Combined sources5
Helixi224 – 226Combined sources3
Helixi230 – 235Combined sources6
Helixi237 – 243Combined sources7
Beta strandi247 – 251Combined sources5
Turni259 – 262Combined sources4
Helixi286 – 288Combined sources3
Helixi296 – 310Combined sources15
Beta strandi314 – 319Combined sources6
Beta strandi328 – 333Combined sources6
Helixi343 – 351Combined sources9
Beta strandi358 – 361Combined sources4
Beta strandi364 – 368Combined sources5
Helixi376 – 391Combined sources16
Beta strandi397 – 400Combined sources4
Helixi403 – 407Combined sources5
Beta strandi411 – 414Combined sources4
Helixi437 – 444Combined sources8
Beta strandi454 – 460Combined sources7
Beta strandi480 – 482Combined sources3
Helixi484 – 495Combined sources12
Helixi504 – 511Combined sources8
Helixi515 – 518Combined sources4
Helixi519 – 521Combined sources3
Helixi525 – 527Combined sources3
Beta strandi528 – 530Combined sources3
Beta strandi535 – 537Combined sources3
Helixi540 – 543Combined sources4
Turni572 – 577Combined sources6
Helixi581 – 597Combined sources17
Beta strandi598 – 605Combined sources8
Helixi608 – 610Combined sources3
Turni626 – 628Combined sources3
Helixi636 – 654Combined sources19
Helixi656 – 658Combined sources3
Turni666 – 668Combined sources3
Beta strandi669 – 672Combined sources4
Beta strandi676 – 678Combined sources3
Helixi681 – 684Combined sources4
Beta strandi691 – 696Combined sources6
Helixi698 – 701Combined sources4
Beta strandi707 – 712Combined sources6
Beta strandi714 – 716Combined sources3
Beta strandi718 – 721Combined sources4
Beta strandi726 – 736Combined sources11
Helixi739 – 741Combined sources3
Beta strandi754 – 758Combined sources5
Beta strandi762 – 765Combined sources4
Beta strandi767 – 776Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BF2X-ray2.00A27-776[»]
ProteinModelPortaliP10342.
SMRiP10342.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10342.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

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.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 4 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P10342-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKCPKILAAL LGCAVLAGVP AMPAHAAINS MSLGASYDAQ QANITFRVYS
60 70 80 90 100
SQATRIVLYL YSAGYGVQES ATYTLSPAGS GVWAVTVPVS SIKAAGITGA
110 120 130 140 150
VYYGYRAWGP NWPYASNWGK GSQAGFVSDV DANGDRFNPN KLLLDPYAQE
160 170 180 190 200
VSQDPLNPSN QNGNVFASGA SYRTTDSGIY APKGVVLVPS TQSTGTKPTR
210 220 230 240 250
AQKDDVIYEV HVRGFTEQDT SIPAQYRGTY YGAGLKASYL ASLGVTAVEF
260 270 280 290 300
LPVQETQNDA NDVVPNSDAN QNYWGYMTEN YFSPDRRYAY NKAAGGPTAE
310 320 330 340 350
FQAMVQAFHN AGIKVYMDVV YNHTAEGGTW TSSDPTTATI YSWRGLDNAT
360 370 380 390 400
YYELTSGNQY FYDNTGIGAN FNTYNTVAQN LIVDSLAYWA NTMGVDGFRF
410 420 430 440 450
DLASVLGNSC LNGAYTASAP NCPNGGYNFD AADSNVAINR ILREFTVRPA
460 470 480 490 500
AGGSGLDLFA EPWAIGGNSY QLGGFPQGWS EWNGLFRDSL RQAQNELGSM
510 520 530 540 550
TIYVTQDAND FSGSSNLFQS SGRSPWNSIN FIDVHDGMTL KDVYSCNGAN
560 570 580 590 600
NSQAWPYGPS DGGTSTNYSW DQGMSAGTGA AVDQRRAART GMAFEMLSAG
610 620 630 640 650
TPLMQGGDEY LRTLQCNNNA YNLDSSANWL TYSWTTDQSN FYTFAQRLIA
660 670 680 690 700
FRKAHPALRP SSWYSGSQLT WYQPSGAVAD SNYWNNTSNY AIAYAINGPS
710 720 730 740 750
LGDSNSIYVA YNGWSSSVTF TLPAPPSGTQ WYRVTDTCDW NDGASTFVAP
760 770
GSETLIGGAG TTYGQCGQSL LLLISK
Length:776
Mass (Da):83,627
Last modified:December 15, 1998 - v3
Checksum:iF738BF8040246169
GO

Sequence cautioni

The sequence AAA25854 differs from that shown. Reason: Frameshift at positions 168, 171, 454, 479, 490, 650 and 662.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8A → G in AAA25854 (PubMed:3379068).Curated1
Sequence conflicti126F → C in AAA25854 (PubMed:3379068).Curated1
Sequence conflicti169G → C in AAA25854 (PubMed:3379068).Curated1
Sequence conflicti386L → V in AAA25854 (PubMed:3379068).Curated1
Sequence conflicti413 – 416GAYT → AVH in AAA25854 (PubMed:3379068).Curated4
Sequence conflicti555 – 556WP → S in AAA25854 (PubMed:3379068).Curated2
Sequence conflicti658 – 661LRPS → SPV in AAA25854 (PubMed:3379068).Curated4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03871 Genomic DNA. Translation: AAA25854.1. Frameshift.
X13378 Genomic DNA. Translation: CAA31754.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03871 Genomic DNA. Translation: AAA25854.1. Frameshift.
X13378 Genomic DNA. Translation: CAA31754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BF2X-ray2.00A27-776[»]
ProteinModelPortaliP10342.
SMRiP10342.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEiP10342.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.68. 5091.

Miscellaneous databases

EvolutionaryTraceiP10342.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 4 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiISOA_PSEAY
AccessioniPrimary (citable) accession number: P10342
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 15, 1998
Last modified: November 2, 2016
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

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