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

Alpha-galactosidase

Gene

galA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes the short-chain alpha-galactosaccharides raffinose, melibiose and stachyose.2 Publications

Catalytic activityi

Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.6 Publications

Enzyme regulationi

Inhibited by hydrolyzation product alpha-galactopyranose and to a lesser extent by beta-galactopyranose, its mutarotational product (PubMed:26005928). Inhibited by synthetic cyclopropyl carbasugars (PubMed:27783466).2 Publications

Kineticsi

kcat is 176 s1 for p-nitrophenol-alpha-galactoside (at pH 5.0 and 75 degrees Celsius). kcat is 109 s1 for raffinose (at pH 5.0 and 75 degrees Celsius) (PubMed:9741105). kcat is 8 s1 for p-nitrophenyl-alpha-D-galactopyranoside (at pH 5.0 and 37 degrees Celsius) (PubMed:24237145). kcat is 2.33 s1 for melibiose (at pH 5.0 and 37 degrees Celsius). kcat is 5.0 s1 for raffinose (at pH 5.0 and 37 degrees Celsius). kcat is 0.53 s1 for stachyose (at pH 5.0 and 37 degrees Celsius) (PubMed:25486100).3 Publications
  1. KM=0.075 mM for p-nitrophenol-alpha-galactoside (at pH 5.0 and 75 degrees Celsius)1 Publication
  2. KM=2.100 mM for raffinose (at pH 5.0 and 75 degrees Celsius)1 Publication
  3. KM=0.110 mM for p-nitrophenyl-alpha-D-galactopyranoside (at pH 5.0 and 37 degrees Celsius)1 Publication
  4. KM=1.170 mM for melibiose (at pH 5.0 and 37 degrees Celsius)1 Publication
  5. KM=10.040 mM for raffinose (at pH 5.0 and 37 degrees Celsius)1 Publication
  6. KM=2.840 mM for stachyose (at pH 5.0 and 37 degrees Celsius)1 Publication
  1. Vmax=166 µmol/min/mg enzyme for 4-nitrophenol-alpha-galactoside (at pH 5.0 and 75 degrees Celsius)1 Publication
  2. Vmax=103 µmol/min/mg enzyme for raffinose (at pH 5.0 and 75 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 5.0-5.5 when using synthetic substrate p-nitrophenyl-alpha-D-galactopyranoside.1 Publication

Temperature dependencei

Optimum temperature is 90-95 degrees Celsius when using synthetic substrate p-nitrophenyl-alpha-D-galactopyranoside. The half-life of thermoinactivation is 6.5 h at 85 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei65SubstrateCombined sources1 Publication1
Binding sitei191SubstrateCombined sources1 Publication1
Active sitei327Nucleophile1 Publication1
Binding sitei368SubstrateCombined sources1 Publication1
Binding sitei383SubstrateCombined sources1 Publication1
Active sitei387Proton donor/proton acceptor1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism

Enzyme and pathway databases

BRENDAi3.2.1.22. 6331.

Protein family/group databases

CAZyiGH36. Glycoside Hydrolase Family 36.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-galactosidase1 PublicationImported (EC:3.2.1.226 Publications)
Alternative name(s):
MelibiaseCurated
Gene namesi
Name:galA1 PublicationImported
Ordered Locus Names:TM_1192Imported
ORF Names:Tmari_1199Imported
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)Imported
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000013901 Componenti: Chromosome
  • UP000008183 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi220D → A: Less than 1% of the wild-type enzyme activity with p-nitrophenyl-alpha-D-galactopyranoside as substrate at 80 degrees Celsius. 1 Publication1
Mutagenesisi220D → G: Reduced activity compared to the wild-type enzyme. 1 Publication1
Mutagenesisi327D → A: Less than 1% of the wild-type enzyme activity with p-nitrophenyl-alpha-D-galactopyranoside as substrate at 80 degrees Celsius. 1 Publication1
Mutagenesisi327D → G: Between 200 and 800-fold lower catalytic rate and between 300 and 1700-fold lower catalytic efficiency than the wild-type enzyme with aryl-alpha-galactosides as substrates. 1 Publication1
Mutagenesisi328F → A: Increased transglycosylating activity at high concentrations of p-nitrophenyl-alpha-D-galactopyranoside substrate, which could be useful in industry and medicine for the synthesis of different p-nitrophenyl-digalactosides. Able to produce 16 times more of a regio-isomer with the (alpha1,2)-bond than wild-type enzyme. 1 Publication1
Mutagenesisi385G → L: Increased transglycosylating activity at high concentrations of p-nitrophenyl-alpha-D-galactopyranoside substrate, which could be useful in industry and medicine for the synthesis of different p-nitrophenyl-digalactosides. 1 Publication1
Mutagenesisi387D → A: Less than 1% of the wild-type enzyme activity with p-nitrophenyl-alpha-D-galactopyranoside as substrate at 80 degrees Celsius. 1 Publication1
Mutagenesisi387D → G: 1500-fold lower catalytic rate and 1000-fold lower catalytic efficiency than the wild-type enzyme with p-nitrophenyl-alpha-D-galactopyranoside as substrate. 1 Publication1
Mutagenesisi402P → D: Increased transglycosylating activity at high concentrations of p-nitrophenyl-alpha-D-galactopyranoside substrate, which could be useful in industry and medicine for the synthesis of different p-nitrophenyl-digalactosides. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004390211 – 552Alpha-galactosidaseAdd BLAST552

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi243274.TM1192.

Structurei

Secondary structure

1552
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 3Combined sources3
Beta strandi10 – 16Combined sources7
Beta strandi18 – 29Combined sources12
Beta strandi32 – 41Combined sources10
Beta strandi45 – 52Combined sources8
Beta strandi55 – 60Combined sources6
Beta strandi68 – 75Combined sources8
Helixi83 – 85Combined sources3
Helixi86 – 89Combined sources4
Helixi93 – 96Combined sources4
Beta strandi99 – 108Combined sources10
Beta strandi111 – 116Combined sources6
Beta strandi119 – 128Combined sources10
Beta strandi131 – 137Combined sources7
Beta strandi143 – 148Combined sources6
Beta strandi152 – 156Combined sources5
Helixi160 – 175Combined sources16
Beta strandi185 – 189Combined sources5
Helixi190 – 193Combined sources4
Helixi194 – 196Combined sources3
Helixi199 – 208Combined sources10
Helixi209 – 211Combined sources3
Beta strandi215 – 219Combined sources5
Beta strandi223 – 226Combined sources4
Helixi240 – 249Combined sources10
Beta strandi253 – 258Combined sources6
Beta strandi262 – 264Combined sources3
Helixi268 – 272Combined sources5
Helixi274 – 276Combined sources3
Beta strandi286 – 290Combined sources5
Beta strandi293 – 298Combined sources6
Helixi303 – 318Combined sources16
Beta strandi323 – 326Combined sources4
Helixi329 – 333Combined sources5
Beta strandi335 – 337Combined sources3
Beta strandi339 – 341Combined sources3
Helixi344 – 359Combined sources16
Beta strandi363 – 367Combined sources5
Helixi373 – 375Combined sources3
Turni376 – 378Combined sources3
Beta strandi380 – 383Combined sources4
Beta strandi398 – 401Combined sources4
Helixi404 – 413Combined sources10
Helixi415 – 417Combined sources3
Turni418 – 420Combined sources3
Beta strandi421 – 425Combined sources5
Beta strandi433 – 435Combined sources3
Helixi440 – 452Combined sources13
Beta strandi457 – 459Combined sources3
Helixi463 – 465Combined sources3
Helixi468 – 478Combined sources11
Beta strandi482 – 487Combined sources6
Turni488 – 491Combined sources4
Beta strandi493 – 504Combined sources12
Beta strandi507 – 514Combined sources8
Turni515 – 518Combined sources4
Beta strandi519 – 524Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZY9X-ray2.34A1-552[»]
5M0XX-ray1.80A1-552[»]
5M12X-ray1.53A1-552[»]
5M16X-ray1.62A1-552[»]
5M1IX-ray1.55A1-552[»]
ProteinModelPortaliG4FEF4.
SMRiG4FEF4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni220 – 221Substrate bindingCombined sources1 Publication2
Regioni325 – 327Substrate bindingCombined sources1 Publication3

Sequence similaritiesi

Belongs to the glycosyl hydrolase 36 family.Curated

Phylogenomic databases

eggNOGiENOG4107R49. Bacteria.
COG3345. LUCA.
KOiK07407.
OMAiILGCGAP.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR011013. Gal_mutarotase_SF_dom.
IPR002252. Glyco_hydro_36.
IPR017853. Glycoside_hydrolase_SF.
PfamiView protein in Pfam
PF02065. Melibiase. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.

Sequencei

Sequence statusi: Complete.

G4FEF4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIFGKTFRE GRFVLKEKNF TVEFAVEKIH LGWKISGRVK GSPGRLEVLR
60 70 80 90 100
TKAPEKVLVN NWQSWGPCRV VDAFSFKPPE IDPNWRYTAS VVPDVLERNL
110 120 130 140 150
QSDYFVAEEG KVYGFLSSKI AHPFFAVEDG ELVAYLEYFD VEFDDFVPLE
160 170 180 190 200
PLVVLEDPNT PLLLEKYAEL VGMENNARVP KHTPTGWCSW YHYFLDLTWE
210 220 230 240 250
ETLKNLKLAK NFPFEVFQID DAYEKDIGDW LVTRGDFPSV EEMAKVIAEN
260 270 280 290 300
GFIPGIWTAP FSVSETSDVF NEHPDWVVKE NGEPKMAYRN WNKKIYALDL
310 320 330 340 350
SKDEVLNWLF DLFSSLRKMG YRYFKIDFLF AGAVPGERKK NITPIQAFRK
360 370 380 390 400
GIETIRKAVG EDSFILGCGS PLLPAVGCVD GMRIGPDTAP FWGEHIEDNG
410 420 430 440 450
APAARWALRN AITRYFMHDR FWLNDPDCLI LREEKTDLTQ KEKELYSYTC
460 470 480 490 500
GVLDNMIIES DDLSLVRDHG KKVLKETLEL LGGRPRVQNI MSEDLRYEIV
510 520 530 540 550
SSGTLSGNVK IVVDLNSREY HLEKEGKSSL KKRVVKREDG RNFYFYEEGE

RE
Length:552
Mass (Da):63,657
Last modified:December 14, 2011 - v1
Checksum:i91C6E6EFA24EA9D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001072 Genomic DNA. Translation: CAA04514.1.
AE000512 Genomic DNA. Translation: AAD36267.1.
CP004077 Genomic DNA. Translation: AGL50123.1.
PIRiE72283.
RefSeqiNP_228997.1. NC_000853.1.
WP_004080136.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36267; AAD36267; TM_1192.
AGL50123; AGL50123; Tmari_1199.
GeneIDi898292.
KEGGitma:TM1192.
tmi:THEMA_08370.
tmm:Tmari_1199.
tmw:THMA_1218.
PATRICi23937326. VBITheMar51294_1210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001072 Genomic DNA. Translation: CAA04514.1.
AE000512 Genomic DNA. Translation: AAD36267.1.
CP004077 Genomic DNA. Translation: AGL50123.1.
PIRiE72283.
RefSeqiNP_228997.1. NC_000853.1.
WP_004080136.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZY9X-ray2.34A1-552[»]
5M0XX-ray1.80A1-552[»]
5M12X-ray1.53A1-552[»]
5M16X-ray1.62A1-552[»]
5M1IX-ray1.55A1-552[»]
ProteinModelPortaliG4FEF4.
SMRiG4FEF4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1192.

Protein family/group databases

CAZyiGH36. Glycoside Hydrolase Family 36.

Protocols and materials databases

DNASUi898292.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36267; AAD36267; TM_1192.
AGL50123; AGL50123; Tmari_1199.
GeneIDi898292.
KEGGitma:TM1192.
tmi:THEMA_08370.
tmm:Tmari_1199.
tmw:THMA_1218.
PATRICi23937326. VBITheMar51294_1210.

Phylogenomic databases

eggNOGiENOG4107R49. Bacteria.
COG3345. LUCA.
KOiK07407.
OMAiILGCGAP.

Enzyme and pathway databases

BRENDAi3.2.1.22. 6331.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR011013. Gal_mutarotase_SF_dom.
IPR002252. Glyco_hydro_36.
IPR017853. Glycoside_hydrolase_SF.
PfamiView protein in Pfam
PF02065. Melibiase. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAGAL_THEMA
AccessioniPrimary (citable) accession number: G4FEF4
Secondary accession number(s): O33835
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2017
Last sequence update: December 14, 2011
Last modified: May 10, 2017
This is version 50 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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

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.