ID   Q9STC1_GRALE            Unreviewed;      1088 AA.
AC   Q9STC1;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
DE   Flags: Fragment;
GN   Name=Ag111 {ECO:0000313|EMBL:CAB51910.1};
OS   Gracilariopsis lemaneiformis (Red alga) (Gracilaria lemaneiformis).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Gracilariopsis.
OX   NCBI_TaxID=2782 {ECO:0000313|EMBL:CAB51910.1};
RN   [1] {ECO:0000313|EMBL:CAB51910.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=10082967; DOI=10.1016/S0167-4838(99)00017-5;
RA   Bojsen K., Yu S., Kragh K.M., Marcussen J.;
RT   "A group of alpha-1,4-glucan lyases and their genes from the red alga
RT   Gracilariopsis lemaneiformis: purification, cloning, and heterologous
RT   expression.";
RL   Biochim. Biophys. Acta 1430:396-402(1999).
RN   [2] {ECO:0007829|PDB:2X2H, ECO:0007829|PDB:2X2I}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 62-1088.
RX   PubMed=23902768; DOI=10.1074/JBC.M113.485896;
RA   Rozeboom H.J., Yu S., Madrid S., Kalk K.H., Zhang R., Dijkstra B.W.;
RT   "Crystal structure of alpha-1,4-glucan lyase, a unique glycoside hydrolase
RT   family member with a novel catalytic mechanism.";
RL   J. Biol. Chem. 288:26764-26774(2013).
CC   -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC       {ECO:0000256|ARBA:ARBA00004833}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; Y18737; CAB51910.1; -; Genomic_DNA.
DR   PDB; 2X2H; X-ray; 2.06 A; A/B/C/D=62-1088.
DR   PDB; 2X2I; X-ray; 2.60 A; A/B/C/D=62-1088.
DR   PDB; 2X2J; X-ray; 2.35 A; A/B/C/D=62-1088.
DR   PDB; 4AMW; X-ray; 1.90 A; A/B/C/D=62-1088.
DR   PDB; 4AMX; X-ray; 2.10 A; A/B/C/D=62-1088.
DR   PDBsum; 2X2H; -.
DR   PDBsum; 2X2I; -.
DR   PDBsum; 2X2J; -.
DR   PDBsum; 4AMW; -.
DR   PDBsum; 4AMX; -.
DR   AlphaFoldDB; Q9STC1; -.
DR   SMR; Q9STC1; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   BioCyc; MetaCyc:MONOMER-19293; -.
DR   BRENDA; 4.2.2.13; 2505.
DR   EvolutionaryTrace; Q9STC1; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0047457; F:exo-(1,4)-alpha-D-glucan lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06601; GH31_lyase_GLase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF54; BCDNA.GH04962; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2X2H, ECO:0007829|PDB:2X2I};
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185};
KW   Lyase {ECO:0000313|EMBL:CAB51910.1}.
FT   DOMAIN          409..825
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          833..932
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAB51910.1"
SQ   SEQUENCE   1088 AA;  122338 MW;  AFA40991350ABEFA CRC64;
     MFSTLAFVAP SALGASTFVG AEVRSNVRIH SAFPAVHTAT RKTNRLNVSM TALSDKQTAT
     AGSTDNPDGI DYKTYDYVGV WGFSPLSNTN WFAAGSSTPG GITDWTATMN VNFDRIDNPS
     ITVQHPVQVQ VTSYNNNSYR VRFNPDGPIR DVTRGPILKQ QLDWIRTQEL SEGCDPGMTF
     TSEGFLTFET KDLSVIIYGN FKTRVTRKSD GKVIMENDEV GTASSGNKCR GLMFVDRLYG
     NAIASVNKNF RNDAVKQEGF YGAGEVNCKY QDTYILERTG IAMTNYNYDN LNYNQWDLRP
     PHHDGALNPD YYIPMYYAAP WLIVNGCAGT SEQYSYGWFM DNVSQSYMNT GDTTWNSGQE
     DLAYMGAQYG PFDQHFVYGA GGGMECVVTA FSLLQGKEFE NQVLNKRSVM PPKYVFGFFQ
     GVFGTSSLLR AHMPAGENNI SVEEIVEGYQ NNNFPFEGLA VDVDMQDNLR VFTTKGEFWT
     ANRVGTGGDP NNRSVFEWAH DKGLVCQTNI TCFLRNDNEG QDYEVNQTLR ERQLYTKNDS
     LTGTDFGMTD DGPSDAYIGH LDYGGGVECD ALFPDWGRPD VAEWWGNNYK KLFSIGLDFV
     WQDMTVPAMM PHKIGDDINV KPDGNWPNAD DPSNGQYNWK TYHPQVLVTD MRYENHGREP
     MVTQRNIHAY TLCESTRKEG IVENADTLTK FRRSYIISRG GYIGNQHFGG MWVGDNSTTS
     NYIQMMIANN INMNMSCLPL VGSDIGGFTS YDNENQRTPC TGDLMVRYVQ AGCLLPWFRN
     HYDRWIESKD HGKDYQELYM YPNEMDTLRK FVEFRYRWQE VLYTAMYQNA AFGKPIIKAA
     SMYNNDSNVR RAQNDHFLLG GHDGYRILCA PVVWENSTER ELYLPVLTQW YKFGPDFDTK
     PLEGAMNGGD RIYNYPVPQS ESPIFVREGA ILPTRYTLNG ENKSLNTYTD EDPLVFEVFP
     LGNNRADGMC YLDDGGVTTN AEDNGKFSVV KVAAEQDGGT ETITFTNDCY EYVFGGPFYV
     RVRGAQSPSN IHVSSGAGSQ DMKVSSATSR AALFNDGENG DFWVDQETDS LWLKLPNVVL
     PDAVITIT
//