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Protein

Alpha-amylase

Gene

amlB

Organism
Streptomyces lividans
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolismUniRule annotation

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylaseUniRule annotation (EC:3.2.1.1UniRule annotation)
Gene namesi
Name:amlBImported
OrganismiStreptomyces lividansImported
Taxonomic identifieri1916 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence analysisAdd
BLAST
Chaini36 – 573538Alpha-amylaseSequence analysisPRO_5004161739Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP97179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini473 – 573101CBM20 (carbohydrate binding type-20)InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.UniRule annotationSAAS annotation

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
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.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 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.

P97179-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHGNTSPARR ITATALALTA GVAGSLLATT APAQASPPGD KDVTAVMFEW
60 70 80 90 100
KFTSVGQACT DTLGPAGYGY VQVSPPQEHI QGGQWWTSYQ PVSYRIAGRL
110 120 130 140 150
GDRAQFKSMV DTCHAAGVKV VADSVVNHMS AGNGTGTGGS SYTKYDYPGL
160 170 180 190 200
YSSNDLDNCT SQINNYGDRF NVQECELVGL ADLDTGEAYV RGKIAGYLTD
210 220 230 240 250
LLSLGVDGFR IDAAKHMAAA DLAAIKSRLS NPNVYWKHEA IYGAGEAVSP
260 270 280 290 300
TEYVGSGDVQ EFRYARDLKR VFNGENLAYL KNFGEAWGHL PSDEAAVFVT
310 320 330 340 350
NHDTERNGET LTYKDGATYT LAHVFMLAWP YGSPDVHSGY EFTDHDAGPP
360 370 380 390 400
NGGQVNACYS DGWKCQHAWR EISSMVAFRN TARGQGVTDW WDNGGDQIAF
410 420 430 440 450
GRGSKAYVAI NHEGTSLTRT FQTSLPAGDY CDVQTGKGVT VDGAGRFTAT
460 470 480 490 500
LGAGTAVALH VGARTCDGGD PGDPDPVSSG VSFAVDATTS WGQDIYVTGN
510 520 530 540 550
RPGLGHWDPG GGLQLDPAAY PVWKRDVELP EGTTFEYKSL RKADAGNVTW
560 570
ESGANRTATV NTTKTTLNDT WRN
Length:573
Mass (Da):61,214
Last modified:May 1, 1997 - v1
Checksum:iE474019661C9D6A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z85949 Genomic DNA. Translation: CAB06622.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z85949 Genomic DNA. Translation: CAB06622.1.

3D structure databases

ProteinModelPortaliP97179.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
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.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterization of a new alpha amylase gene from Streptomyces lividans TK 24."
    Yin X.H., Gagnat J., Gerbaud C., Guerineau M., Virolle M.J.
    Gene 1997:37-45(1997)
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiP97179_STRLI
AccessioniPrimary (citable) accession number: P97179
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1997
Last sequence update: May 1, 1997
Last modified: May 11, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.