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P10342

- ISOA_PSEAY

UniProt

P10342 - ISOA_PSEAY

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Protein

Isoamylase

Gene

iam

Organism
Pseudomonas amyloderamosa
Status
Reviewed - 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.

Cofactori

Ca2+Note: Binds 1 Ca(2+) ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi154 – 1541Calcium
Metal bindingi255 – 2551Calcium
Metal bindingi256 – 2561Calcium; via carbonyl oxygen
Metal bindingi258 – 2581Calcium
Metal bindingi285 – 2851Calcium
Active sitei401 – 4011Nucleophile
Active sitei461 – 4611Proton donor
Sitei536 – 5361Transition state stabilizerBy similarity

GO - Molecular functioni

  1. isoamylase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Isoamylase (EC:3.2.1.68)
Gene namesi
Name:iam
OrganismiPseudomonas amyloderamosa
Taxonomic identifieri32043 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Add
BLAST
Chaini27 – 776750IsoamylasePRO_0000001424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi410 ↔ 422
Disulfide bondi546 ↔ 616
Disulfide bondi738 ↔ 766

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By maltose.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
776
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 374Combined sources
Beta strandi41 – 499Combined sources
Beta strandi54 – 6613Combined sources
Beta strandi70 – 745Combined sources
Beta strandi82 – 887Combined sources
Helixi89 – 946Combined sources
Beta strandi102 – 1098Combined sources
Helixi163 – 1664Combined sources
Turni170 – 1745Combined sources
Turni178 – 1803Combined sources
Helixi202 – 2043Combined sources
Beta strandi207 – 2104Combined sources
Helixi212 – 2165Combined sources
Helixi224 – 2263Combined sources
Helixi230 – 2356Combined sources
Helixi237 – 2437Combined sources
Beta strandi247 – 2515Combined sources
Turni259 – 2624Combined sources
Helixi286 – 2883Combined sources
Helixi296 – 31015Combined sources
Beta strandi314 – 3196Combined sources
Beta strandi328 – 3336Combined sources
Helixi343 – 3519Combined sources
Beta strandi358 – 3614Combined sources
Beta strandi364 – 3685Combined sources
Helixi376 – 39116Combined sources
Beta strandi397 – 4004Combined sources
Helixi403 – 4075Combined sources
Beta strandi411 – 4144Combined sources
Helixi437 – 4448Combined sources
Beta strandi454 – 4607Combined sources
Beta strandi480 – 4823Combined sources
Helixi484 – 49512Combined sources
Helixi504 – 5118Combined sources
Helixi515 – 5184Combined sources
Helixi519 – 5213Combined sources
Helixi525 – 5273Combined sources
Beta strandi528 – 5303Combined sources
Beta strandi535 – 5373Combined sources
Helixi540 – 5434Combined sources
Turni572 – 5776Combined sources
Helixi581 – 59717Combined sources
Beta strandi598 – 6058Combined sources
Helixi608 – 6103Combined sources
Turni626 – 6283Combined sources
Helixi636 – 65419Combined sources
Helixi656 – 6583Combined sources
Turni666 – 6683Combined sources
Beta strandi669 – 6724Combined sources
Beta strandi676 – 6783Combined sources
Helixi681 – 6844Combined sources
Beta strandi691 – 6966Combined sources
Helixi698 – 7014Combined sources
Beta strandi707 – 7126Combined sources
Beta strandi714 – 7163Combined sources
Beta strandi718 – 7214Combined sources
Beta strandi726 – 73611Combined sources
Helixi739 – 7413Combined sources
Beta strandi754 – 7585Combined sources
Beta strandi762 – 7654Combined sources
Beta strandi767 – 77610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BF2X-ray2.00A27-776[»]
ProteinModelPortaliP10342.
SMRiP10342. Positions 27-776.
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.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 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 AAA25854.1 differs from that shown. Reason: Frameshift at positions 168, 171, 454, 479, 490, 650 and 662. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81A → G in AAA25854. (PubMed:3379068)Curated
Sequence conflicti126 – 1261F → C in AAA25854. (PubMed:3379068)Curated
Sequence conflicti169 – 1691G → C in AAA25854. (PubMed:3379068)Curated
Sequence conflicti386 – 3861L → V in AAA25854. (PubMed:3379068)Curated
Sequence conflicti413 – 4164GAYT → AVH in AAA25854. (PubMed:3379068)Curated
Sequence conflicti555 – 5562WP → S in AAA25854. (PubMed:3379068)Curated
Sequence conflicti658 – 6614LRPS → SPV in AAA25854. (PubMed:3379068)Curated

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
Entry Method Resolution (Å) Chain Positions PDBsum
1BF2 X-ray 2.00 A 27-776 [» ]
ProteinModelPortali P10342.
SMRi P10342. Positions 27-776.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P10342.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Cloning and nucleotide sequence of the isoamylase gene from Pseudomonas amyloderamosa SB-15."
    Amemura A., Chakraborty R., Fujita M., Noumi T., Futai M.
    J. Biol. Chem. 263:9271-9275(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SB-15.
  2. "Nucleotide sequence and expression of the isoamylase gene from an isoamylase-hyperproducing mutant, Pseudomonas amyloderamosa JD210."
    Chen J.H., Chen Z.Y., Chow T.Y., Chen J.C., Tan S.T., Hsu W.H.
    Biochim. Biophys. Acta 1087:309-315(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: JD210.
  3. "Transcription of the isoamylase gene (iam) in Pseudomonas amyloderamosa SB-15."
    Amemura A., Fujita M., Futai M.
    J. Bacteriol. 171:4320-4325(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 744-776.
    Strain: SB-15.
  4. "Three-dimensional structure of Pseudomonas isoamylase at 2.2-A resolution."
    Katsuya Y., Mezaki Y., Kubota M., Matsuura Y.
    J. Mol. Biol. 281:885-897(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

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 26, 2014
This is version 99 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

External Data

Dasty 3