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Protein

4-alpha-glucanotransferase

Gene

malQ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 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)DescriptionActionsGraphical viewLength
ChainiPRO_00001701251 – 6944-alpha-glucanotransferaseAdd BLAST694

Proteomic databases

EPDiP15977.
PaxDbiP15977.
PRIDEiP15977.

Interactioni

Protein-protein interaction databases

BioGridi4261216. 124 interactors.
DIPiDIP-10147N.
IntActiP15977. 6 interactors.
MINTiMINT-1275716.
STRINGi511145.b3416.

Structurei

Secondary structure

1694
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 12Combined sources9
Beta strandi17 – 20Combined sources4
Beta strandi26 – 28Combined sources3
Helixi31 – 40Combined sources10
Beta strandi56 – 61Combined sources6
Beta strandi67 – 69Combined sources3
Beta strandi72 – 81Combined sources10
Beta strandi83 – 85Combined sources3
Beta strandi87 – 93Combined sources7
Beta strandi97 – 99Combined sources3
Beta strandi106 – 117Combined sources12
Beta strandi119 – 127Combined sources9
Helixi135 – 138Combined sources4
Beta strandi143 – 148Combined sources6
Helixi150 – 152Combined sources3
Beta strandi156 – 161Combined sources6
Helixi164 – 176Combined sources13
Beta strandi181 – 185Combined sources5
Beta strandi204 – 209Combined sources6
Helixi211 – 213Combined sources3
Helixi216 – 218Combined sources3
Helixi220 – 224Combined sources5
Helixi226 – 232Combined sources7
Helixi235 – 246Combined sources12
Beta strandi247 – 249Combined sources3
Helixi252 – 270Combined sources19
Helixi276 – 308Combined sources33
Helixi315 – 317Combined sources3
Helixi320 – 322Combined sources3
Helixi328 – 336Combined sources9
Helixi338 – 364Combined sources27
Beta strandi368 – 375Combined sources8
Helixi384 – 388Combined sources5
Helixi390 – 392Combined sources3
Beta strandi397 – 401Combined sources5
Beta strandi405 – 407Combined sources3
Beta strandi411 – 415Combined sources5
Helixi420 – 425Combined sources6
Turni426 – 428Combined sources3
Helixi429 – 438Combined sources10
Beta strandi443 – 447Combined sources5
Helixi450 – 453Combined sources4
Beta strandi455 – 460Combined sources6
Helixi465 – 467Combined sources3
Beta strandi469 – 472Combined sources4
Helixi475 – 489Combined sources15
Beta strandi492 – 495Combined sources4
Helixi503 – 511Combined sources9
Beta strandi515 – 519Combined sources5
Helixi520 – 522Combined sources3
Helixi533 – 535Combined sources3
Beta strandi538 – 544Combined sources7
Helixi552 – 556Combined sources5
Helixi559 – 566Combined sources8
Helixi573 – 596Combined sources24
Beta strandi602 – 604Combined sources3
Helixi608 – 610Combined sources3
Helixi615 – 626Combined sources12
Beta strandi631 – 635Combined sources5
Helixi637 – 640Combined sources4
Turni654 – 659Combined sources6
Beta strandi664 – 666Combined sources3
Helixi667 – 670Combined sources4
Helixi674 – 688Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4S3PX-ray2.80A/B1-688[»]
4S3QX-ray2.10A/B/C1-688[»]
4S3RX-ray2.10A1-688[»]
ProteinModelPortaliP15977.
SMRiP15977.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the disproportionating enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4107RTM. Bacteria.
COG1640. LUCA.
HOGENOMiHOG000245168.
InParanoidiP15977.
KOiK00705.
OMAiWSRQDEL.
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)DescriptionActionsGraphical viewLength
Sequence conflicti22A → P in AAA24106 (PubMed:2845225).Curated1
Sequence conflicti199 – 200SP → TA in AAA24106 (PubMed:2845225).Curated2
Sequence conflicti380 – 381AE → GT in AAA24106 (PubMed:2845225).Curated2
Sequence conflicti462G → R in AAA24106 (PubMed:2845225).Curated1

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.
WP_000444342.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76441; AAC76441; b3416.
BAE77875; BAE77875; BAE77875.
GeneIDi947923.
KEGGiecj:JW3379.
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.
WP_000444342.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4S3PX-ray2.80A/B1-688[»]
4S3QX-ray2.10A/B/C1-688[»]
4S3RX-ray2.10A1-688[»]
ProteinModelPortaliP15977.
SMRiP15977.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261216. 124 interactors.
DIPiDIP-10147N.
IntActiP15977. 6 interactors.
MINTiMINT-1275716.
STRINGi511145.b3416.

Protein family/group databases

CAZyiGH77. Glycoside Hydrolase Family 77.

Proteomic databases

EPDiP15977.
PaxDbiP15977.
PRIDEiP15977.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76441; AAC76441; b3416.
BAE77875; BAE77875; BAE77875.
GeneIDi947923.
KEGGiecj:JW3379.
eco:b3416.
PATRICi32122270. VBIEscCol129921_3512.

Organism-specific databases

EchoBASEiEB0556.
EcoGeneiEG10561. malQ.

Phylogenomic databases

eggNOGiENOG4107RTM. Bacteria.
COG1640. LUCA.
HOGENOMiHOG000245168.
InParanoidiP15977.
KOiK00705.
OMAiWSRQDEL.
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...

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: November 2, 2016
This is version 135 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

3D-structure, Complete proteome, Reference proteome

Documents

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