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Protein

Maltase A1

Gene

Mal-A1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei221 – 2211NucleophileBy similarity
Active sitei297 – 2971Proton donorBy similarity
Sitei363 – 3631Transition state stabilizerBy similarity

GO - Molecular functioni

  1. alpha-1,4-glucosidase activity Source: UniProtKB-EC
  2. cation binding Source: InterPro
  3. maltose alpha-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

ReactomeiREACT_254974. Amino acid transport across the plasma membrane.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Maltase A1 (EC:3.2.1.20)
Alternative name(s):
Larval visceral protein H
Gene namesi
Name:Mal-A1
Synonyms:LvpH
ORF Names:CG8696
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0002570. Mal-A1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 577558Maltase A1PRO_0000001447Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP07190.
PRIDEiP07190.

Expressioni

Developmental stagei

One of the proteins expressed by the 44D cuticle gene cluster. Expressed in first, second and early 3rd instar larvae and in adults, but not in embryos or pupae.1 Publication

Gene expression databases

BgeeiP07190.

Interactioni

Protein-protein interaction databases

BioGridi61676. 5 interactions.
IntActiP07190. 1 interaction.
MINTiMINT-1599685.
STRINGi7227.FBpp0087838.

Structurei

3D structure databases

ProteinModelPortaliP07190.
SMRiP07190. Positions 19-575.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0366.
GeneTreeiENSGT00530000063127.
InParanoidiP07190.
KOiK01187.
OMAiDVLWLNP.
OrthoDBiEOG7B31NK.
PhylomeDBiP07190.

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P07190-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRPQSAACLL LAIVGFVGAT EWWESGNYYQ IYPRSFRDSD GDGIGDLNGV
60 70 80 90 100
TEKLQYLKDI GFTGTWLSPI FKSPMVDFGY DISDFYQIHP EYGTMEDFER
110 120 130 140 150
MIAKAKEVGI KIILDFVPNH SSTENEWFTK SVDSDPVYKD FYIWHDGKIN
160 170 180 190 200
NETGEREPPS NWNSEFRYSA WEWNEVRQQY YLHQFAIQQA DLNYRNPAVV
210 220 230 240 250
NEMKNVIRFW LGKGVSGFRI DAVPYLFEVD LDRYNQYPDE PLTNDSVNCP
260 270 280 290 300
DPDDHCYTQH IYTQDMPETI DMVYQWRELV DEFHVENGGD KRLLMTEAYT
310 320 330 340 350
SFENIMTYYG NGVRNGSHIP FNFDFLTSIN NASKAGEYVE HIKKWMDAMP
360 370 380 390 400
EGVYANWVLG NHDNKRVASR FGVQRTDLIN ILLQTLPGHA VTYNGEELGM
410 420 430 440 450
TDVWISWEDT VDPNACNSDP DNYYARSRDP ARSPYQWDAS SKAGFTSADH
460 470 480 490 500
TWLPVADDYK TNNALQQLRA PRSHLQIFKK LVRVRKEPSF RQGELNIQAI
510 520 530 540 550
DDDVIIYSRQ KTGSDLYVIV LNLGSTSKTL DLTKYYELGT QAEVITTSLS
560 570
SQYIDGDVIK STEFVANPYV GTVLVAV
Length:577
Mass (Da):66,386
Last modified:February 2, 2004 - v2
Checksum:iE005AE05F98ABE0F
GO

Sequence cautioni

The sequence AAL48097.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00204 Genomic DNA. Translation: CAA23491.1. Sequence problems.
AE013599 Genomic DNA. Translation: AAF59089.3.
AY070626 mRNA. Translation: AAL48097.2. Different initiation.
PIRiS07253.
RefSeqiNP_476627.3. NM_057279.5.

Genome annotation databases

EnsemblMetazoaiFBtr0088759; FBpp0087838; FBgn0002570.
GeneIDi35824.
KEGGidme:Dmel_CG8696.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00204 Genomic DNA. Translation: CAA23491.1. Sequence problems.
AE013599 Genomic DNA. Translation: AAF59089.3.
AY070626 mRNA. Translation: AAL48097.2. Different initiation.
PIRiS07253.
RefSeqiNP_476627.3. NM_057279.5.

3D structure databases

ProteinModelPortaliP07190.
SMRiP07190. Positions 19-575.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61676. 5 interactions.
IntActiP07190. 1 interaction.
MINTiMINT-1599685.
STRINGi7227.FBpp0087838.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbiP07190.
PRIDEiP07190.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088759; FBpp0087838; FBgn0002570.
GeneIDi35824.
KEGGidme:Dmel_CG8696.

Organism-specific databases

CTDi35824.
FlyBaseiFBgn0002570. Mal-A1.

Phylogenomic databases

eggNOGiCOG0366.
GeneTreeiENSGT00530000063127.
InParanoidiP07190.
KOiK01187.
OMAiDVLWLNP.
OrthoDBiEOG7B31NK.
PhylomeDBiP07190.

Enzyme and pathway databases

ReactomeiREACT_254974. Amino acid transport across the plasma membrane.

Miscellaneous databases

GenomeRNAii35824.
NextBioi795387.

Gene expression databases

BgeeiP07190.

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two gene families clustered in a small region of the Drosophila genome."
    Snyder M., Davidson N.
    J. Mol. Biol. 166:101-118(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. Cited for: SEQUENCE REVISION.

Entry informationi

Entry nameiMAL1_DROME
AccessioniPrimary (citable) accession number: P07190
Secondary accession number(s): Q9V4T6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 2, 2004
Last modified: January 7, 2015
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.