Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

4-alpha-glucanotransferase

Gene

malQ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.

GO - Molecular functioni

  • 4-alpha-glucanotransferase activity Source: EcoCyc

GO - Biological processi

  • glycogen metabolic process Source: GOC
  • maltose catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciEcoCyc:AMYLOMALT-MONOMER.
ECOL316407:JW3379-MONOMER.
MetaCyc:AMYLOMALT-MONOMER.

Protein family/group databases

CAZyiGH77. Glycoside Hydrolase Family 77.

Names & Taxonomyi

Protein namesi
Recommended name:
4-alpha-glucanotransferase (EC:2.4.1.25)
Alternative name(s):
Amylomaltase
Disproportionating enzyme
Short name:
D-enzyme
Gene namesi
Name:malQ
Synonyms:malA
Ordered Locus Names:b3416, JW3379
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10561. malQ.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6946944-alpha-glucanotransferasePRO_0000170125Add
BLAST

Proteomic databases

PaxDbiP15977.
PRIDEiP15977.

Interactioni

Protein-protein interaction databases

DIPiDIP-10147N.
IntActiP15977. 6 interactions.
MINTiMINT-1275716.
STRINGi511145.b3416.

Structurei

3D structure databases

ProteinModelPortaliP15977.
SMRiP15977. Positions 155-213, 250-556.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the disproportionating enzyme family.Curated

Phylogenomic databases

eggNOGiCOG1640.
HOGENOMiHOG000245168.
InParanoidiP15977.
KOiK00705.
OMAiWSRQDEL.
OrthoDBiEOG6SR926.
PhylomeDBiP15977.

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR003385. Glyco_hydro_77.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02446. Glyco_hydro_77. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
TIGRFAMsiTIGR00217. malQ. 1 hit.

Sequencei

Sequence statusi: Complete.

P15977-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESKRLDNAA LAAGISPNYI NAHGKPQSIS AETKRRLLDA MHQRTATKVA
60 70 80 90 100
VTPVPNVMVY TSGKKMPMVV EGSGEYSWLL TTEEGTQYKG HVTGGKAFNL
110 120 130 140 150
PTKLPEGYHT LTLTQDDQRA HCRVIVAPKR CYEPQALLNK QKLWGACVQL
160 170 180 190 200
YTLRSEKNWG IGDFGDLKAM LVDVAKRGGS FIGLNPIHAL YPANPESASP
210 220 230 240 250
YSPSSRRWLN VIYIDVNAVE DFHLSEEAQA WWQLPTTQQT LQQARDADWV
260 270 280 290 300
DYSTVTALKM TALRMAWKGF AQRDDEQMAA FRQFVAEQGD SLFWQAAFDA
310 320 330 340 350
LHAQQVKEDE MRWGWPAWPE MYQNVDSPEV RQFCEEHRDD VDFYLWLQWL
360 370 380 390 400
AYSQFAACWE ISQGYEMPIG LYRDLAVGVA EGGAETWCDR ELYCLKASVG
410 420 430 440 450
APPDILGPLG QNWGLPPMDP HIITARAYEP FIELLRANMQ NCGALRIDHV
460 470 480 490 500
MSMLRLWWIP YGETADQGAY VHYPVDDLLS ILALESKRHR CMVIGEDLGT
510 520 530 540 550
VPVEIVGKLR SSGVYSYKVL YFENDHEKTF RAPKAYPEQS MAVAATHDLP
560 570 580 590 600
TLRGYWECGD LTLGKTLGLY PDEVVLRGLY QDRELAKQGL LDALHKYGCL
610 620 630 640 650
PKRAGHKASL MSMTPTLNRG LQRYIADSNS ALLGLQPEDW LDMAEPVNIP
660 670 680 690
GTSYQYKNWR RKLSATLESM FADDGVNKLL KDLDRRRRAA AKKK
Length:694
Mass (Da):78,503
Last modified:November 1, 1995 - v2
Checksum:i73FFB3F8E5619311
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221A → P in AAA24106 (PubMed:2845225).Curated
Sequence conflicti199 – 2002SP → TA in AAA24106 (PubMed:2845225).Curated
Sequence conflicti380 – 3812AE → GT in AAA24106 (PubMed:2845225).Curated
Sequence conflicti462 – 4621G → R in AAA24106 (PubMed:2845225).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32793 Genomic DNA. Translation: AAA24106.1.
U18997 Genomic DNA. Translation: AAA58214.1.
U00096 Genomic DNA. Translation: AAC76441.1.
AP009048 Genomic DNA. Translation: BAE77875.1.
PIRiC65137.
RefSeqiNP_417875.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76441; AAC76441; b3416.
BAE77875; BAE77875; BAE77875.
GeneIDi947923.
KEGGiecj:Y75_p3760.
eco:b3416.
PATRICi32122270. VBIEscCol129921_3512.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32793 Genomic DNA. Translation: AAA24106.1.
U18997 Genomic DNA. Translation: AAA58214.1.
U00096 Genomic DNA. Translation: AAC76441.1.
AP009048 Genomic DNA. Translation: BAE77875.1.
PIRiC65137.
RefSeqiNP_417875.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP15977.
SMRiP15977. Positions 155-213, 250-556.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10147N.
IntActiP15977. 6 interactions.
MINTiMINT-1275716.
STRINGi511145.b3416.

Protein family/group databases

CAZyiGH77. Glycoside Hydrolase Family 77.

Proteomic databases

PaxDbiP15977.
PRIDEiP15977.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76441; AAC76441; b3416.
BAE77875; BAE77875; BAE77875.
GeneIDi947923.
KEGGiecj:Y75_p3760.
eco:b3416.
PATRICi32122270. VBIEscCol129921_3512.

Organism-specific databases

EchoBASEiEB0556.
EcoGeneiEG10561. malQ.

Phylogenomic databases

eggNOGiCOG1640.
HOGENOMiHOG000245168.
InParanoidiP15977.
KOiK00705.
OMAiWSRQDEL.
OrthoDBiEOG6SR926.
PhylomeDBiP15977.

Enzyme and pathway databases

BioCyciEcoCyc:AMYLOMALT-MONOMER.
ECOL316407:JW3379-MONOMER.
MetaCyc:AMYLOMALT-MONOMER.

Miscellaneous databases

PROiP15977.

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR003385. Glyco_hydro_77.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02446. Glyco_hydro_77. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
TIGRFAMsiTIGR00217. malQ. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase."
    Pugsley A.P., Dubreuil C.
    Mol. Microbiol. 2:473-479(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiMALQ_ECOLI
AccessioniPrimary (citable) accession number: P15977
Secondary accession number(s): Q2M781
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.