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Protein

Sucrose phosphorylase

Gene
N/A
Organism
Leuconostoc mesenteroides
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate.

GO - Molecular functioni

  1. cation binding Source: InterPro
  2. sucrose phosphorylase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Sucrose phosphorylase (EC:2.4.1.7)
Alternative name(s):
Sucrose glucosyltransferase
OrganismiLeuconostoc mesenteroides
Taxonomic identifieri1245 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLeuconostocaceaeLeuconostoc

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490Sucrose phosphorylasePRO_0000072300Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliQ59495.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sucrose phosphorylase family.Curated

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR016377. Sucrose_phosphorylase.
IPR022527. Sucrose_phosphorylase_GftA.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
PIRSFiPIRSF003059. Sucrose_phosphorylase. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR03852. sucrose_gtfA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q59495-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEIQNKAMLI TYADSLGKNL KDVHQVLKED IGDAIGGVHL LPFFPSTGDR
60 70 80 90 100
GFAPADYTRV DAAFGDWADV EALGEEYYLM FDFMINHISR ESVMYQDFKK
110 120 130 140 150
NHDDSKYKDF FIRWEKFWAK AGENRPTQAD VDLIYKRKDK APTQEITFDD
160 170 180 190 200
GTTENLWNTF GEEQIDIDVN SAIAKEFIKT TLEDMVKHGA NLIRLDAFAY
210 220 230 240 250
AVKKVDTNDF FVEPEIWDTL NEVREILTPL KAEILPEIHE HYSIPKKIND
260 270 280 290 300
HGYFTYDFAL PMTTLYTLYS GKTNQLAKWL KMSPMKQFTT LDTHDGIGVV
310 320 330 340 350
DARDILTDDE IDYASEQLYK VGANVKKTYS SASYNNLDIY QINSTYYSAL
360 370 380 390 400
GNDDAAYLLS RVFQVFAPGI PQIYYVGLLA GENDIALLES TKEGRNINRH
410 420 430 440 450
YYTREEVKSE VKRPVVANLL KLLSWRNESP AFDLAGSITV DTPTDTTIVV
460 470 480 490
TRQDENGQNK AVLTADAANK TFEIVENGQT VMSSDNLTQN
Length:490
Mass (Da):55,743
Last modified:November 1, 1996 - v1
Checksum:i841CCC244CA917BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90314 Genomic DNA. Translation: BAA14344.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90314 Genomic DNA. Translation: BAA14344.1.

3D structure databases

ProteinModelPortaliQ59495.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR016377. Sucrose_phosphorylase.
IPR022527. Sucrose_phosphorylase_GftA.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
PIRSFiPIRSF003059. Sucrose_phosphorylase. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR03852. sucrose_gtfA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Kitao S., Koga T., Nakano E.
    Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Purification and some properties of sucrose phosphorylase from Leuconostoc mesenteroides."
    Koga T., Nakamura K., Shirokane Y., Mizusawa K., Kitao S., Kikuchi M.
    Agric. Biol. Chem. 55:1805-1810(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiSUCP_LEUME
AccessioniPrimary (citable) accession number: Q59495
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: October 1, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. 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.