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Protein
Submitted name:

Alpha-1,4-glucan lyase isozyme 1

Gene

Ag111

Organism
Gracilariopsis lemaneiformis
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. exo-(1,4)-alpha-D-glucan lyase activity Source: UniProtKB-EC
  3. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase, LyaseImported

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Names & Taxonomyi

Protein namesi
Submitted name:
Alpha-1,4-glucan lyase isozyme 1Imported (EC:4.2.2.13Imported)
Gene namesi
Name:Ag111Imported
OrganismiGracilariopsis lemaneiformisImported
Taxonomic identifieri2782 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaFlorideophyceaeGracilarialesGracilariaceaeGracilariopsis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 50›50 PotentialImportedAdd
BLAST
Chaini51 – 10881038 PotentialImportedPRO_5000147347Add
BLAST

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X2HX-ray2.06A/B/C/D62-1088[»]
2X2IX-ray2.60A/B/C/D62-1088[»]
2X2JX-ray2.35A/B/C/D62-1088[»]
4AMWX-ray1.90A/B/C/D62-1088[»]
4AMXX-ray2.10A/B/C/D62-1088[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9STC1.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.UniRule annotation

Keywords - Domaini

SignalImported

Family and domain databases

InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.

Sequencei

Sequence statusi: Fragment.

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

Q9STC1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFSTLAFVAP SALGASTFVG AEVRSNVRIH SAFPAVHTAT RKTNRLNVSM
60 70 80 90 100
TALSDKQTAT AGSTDNPDGI DYKTYDYVGV WGFSPLSNTN WFAAGSSTPG
110 120 130 140 150
GITDWTATMN VNFDRIDNPS ITVQHPVQVQ VTSYNNNSYR VRFNPDGPIR
160 170 180 190 200
DVTRGPILKQ QLDWIRTQEL SEGCDPGMTF TSEGFLTFET KDLSVIIYGN
210 220 230 240 250
FKTRVTRKSD GKVIMENDEV GTASSGNKCR GLMFVDRLYG NAIASVNKNF
260 270 280 290 300
RNDAVKQEGF YGAGEVNCKY QDTYILERTG IAMTNYNYDN LNYNQWDLRP
310 320 330 340 350
PHHDGALNPD YYIPMYYAAP WLIVNGCAGT SEQYSYGWFM DNVSQSYMNT
360 370 380 390 400
GDTTWNSGQE DLAYMGAQYG PFDQHFVYGA GGGMECVVTA FSLLQGKEFE
410 420 430 440 450
NQVLNKRSVM PPKYVFGFFQ GVFGTSSLLR AHMPAGENNI SVEEIVEGYQ
460 470 480 490 500
NNNFPFEGLA VDVDMQDNLR VFTTKGEFWT ANRVGTGGDP NNRSVFEWAH
510 520 530 540 550
DKGLVCQTNI TCFLRNDNEG QDYEVNQTLR ERQLYTKNDS LTGTDFGMTD
560 570 580 590 600
DGPSDAYIGH LDYGGGVECD ALFPDWGRPD VAEWWGNNYK KLFSIGLDFV
610 620 630 640 650
WQDMTVPAMM PHKIGDDINV KPDGNWPNAD DPSNGQYNWK TYHPQVLVTD
660 670 680 690 700
MRYENHGREP MVTQRNIHAY TLCESTRKEG IVENADTLTK FRRSYIISRG
710 720 730 740 750
GYIGNQHFGG MWVGDNSTTS NYIQMMIANN INMNMSCLPL VGSDIGGFTS
760 770 780 790 800
YDNENQRTPC TGDLMVRYVQ AGCLLPWFRN HYDRWIESKD HGKDYQELYM
810 820 830 840 850
YPNEMDTLRK FVEFRYRWQE VLYTAMYQNA AFGKPIIKAA SMYNNDSNVR
860 870 880 890 900
RAQNDHFLLG GHDGYRILCA PVVWENSTER ELYLPVLTQW YKFGPDFDTK
910 920 930 940 950
PLEGAMNGGD RIYNYPVPQS ESPIFVREGA ILPTRYTLNG ENKSLNTYTD
960 970 980 990 1000
EDPLVFEVFP LGNNRADGMC YLDDGGVTTN AEDNGKFSVV KVAAEQDGGT
1010 1020 1030 1040 1050
ETITFTNDCY EYVFGGPFYV RVRGAQSPSN IHVSSGAGSQ DMKVSSATSR
1060 1070 1080
AALFNDGENG DFWVDQETDS LWLKLPNVVL PDAVITIT
Length:1,088
Mass (Da):122,338
Last modified:May 1, 2000 - v1
Checksum:iAFA40991350ABEFA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18737 Genomic DNA. Translation: CAB51910.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18737 Genomic DNA. Translation: CAB51910.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X2HX-ray2.06A/B/C/D62-1088[»]
2X2IX-ray2.60A/B/C/D62-1088[»]
2X2JX-ray2.35A/B/C/D62-1088[»]
4AMWX-ray1.90A/B/C/D62-1088[»]
4AMXX-ray2.10A/B/C/D62-1088[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9STC1.

Family and domain databases

InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "A group of alpha-1,4-glucan lyases and their genes from the red alga Gracilariopsis lemaneiformis: purification, cloning, and heterologous expression."
    Bojsen K., Yu S., Kragh K.M., Marcussen J.
    Biochim. Biophys. Acta 1430:396-402(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Crystal structure of ?-1,4-glucan lyase, a unique glycoside hydrolase family member with a novel catalytic mechanism."
    Rozeboom H.J., Yu S., Madrid S., Kalk K.H., Zhang R., Dijkstra B.W.
    J. Biol. Chem. 288:26764-26774(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 62-1088.

Entry informationi

Entry nameiQ9STC1_9FLOR
AccessioniPrimary (citable) accession number: Q9STC1
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: January 7, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.