ID A8B231_GIAIC Unreviewed; 1215 AA.
AC A8B231;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00012560};
DE EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560};
DE AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423};
DE AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501};
GN ORFNames=GL50803_8978 {ECO:0000313|EMBL:EDO82214.1};
OS Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=184922 {ECO:0000313|EMBL:EDO82214.1};
RN [1] {ECO:0000313|EMBL:EDO82214.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB C6 {ECO:0000313|EMBL:EDO82214.1};
RX PubMed=17901334; DOI=10.1126/science.1143837;
RA Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E., Palm D.,
RA Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA Svard S.G., Sogin M.L.;
RT "Genomic minimalism in the early diverging intestinal parasite Giardia
RT lamblia.";
RL Science 317:1921-1926(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC glucan.; EC=2.4.1.25; Evidence={ECO:0000256|ARBA:ARBA00000439};
CC -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC {ECO:0000256|ARBA:ARBA00005684}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDO82214.1}.
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DR EMBL; AACB02000001; EDO82214.1; -; Genomic_DNA.
DR RefSeq; XP_001709888.1; XM_001709836.1.
DR AlphaFoldDB; A8B231; -.
DR STRING; 184922.A8B231; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH77; Glycoside Hydrolase Family 77.
DR EnsemblProtists; EDO82214; EDO82214; GL50803_8978.
DR GeneID; 5702812; -.
DR KEGG; gla:GL50803_008978; -.
DR VEuPathDB; GiardiaDB:GL50803_8978; -.
DR HOGENOM; CLU_269309_0_0_1; -.
DR OMA; KYRIHIS; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR32518; -; 1.
DR PANTHER; PTHR32518:SF3; 4-ALPHA-GLUCANOTRANSFERASE; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF02446; Glyco_hydro_77; 2.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosyltransferase {ECO:0000313|EMBL:EDO82214.1};
KW Transferase {ECO:0000313|EMBL:EDO82214.1}.
FT DOMAIN 251..359
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 386..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1215 AA; 138095 MW; 16463B3EAB1356D4 CRC64;
MSFIFPLQLL YKAGRKTMDH ALRVNIRFVV DNYVAHPTQR LALLSSFAKE PMVFMRRNGP
LWELDLDITD TLERLSEDRA DTEDMRAYRY AVINEDGSQS PDVLKRILPN IPPTQSIYDQ
CISALVLHPQ YESLVNNSGN VLDVSFTLVD DWSFSSSSPW NTSAMKVMIG HDLKVDKSVL
DSGHLLNKLF NRCFWKIDDS LDMTDSATTS ILKDATIHHG APEKLAILKV SKVVKEVENK
KAIAKLSRSN LVQSNLVPVL FACMVPYVFK GERVLLTGNL PRFGNWNPRS RSSIIFNHVG
ERRFEAPTVF YFTVDELKTF LFKFAIVHAD GNISFESGEN RSIHLSETFS MTATYTLGDE
SVHRTLPYKT VGDLYAAAAA SATTSTTTTA SSPGQKDDQE VEDNNNSSEV KLLSSAPSTA
KKGNSHLKTV TIRYWSYFIC GFFRYPYSAV PRFTSLCVPL FSLRSALSTG VGDFGDLRML
VNFAKCCGFN IIQLLPLQDT ITGPILSPSG TNTIKSHFSA GDSSPYAGIS VFALHPIYIR
CEKISGMDSV VTRKLNDFRH HMTRDISYLH CRYNYGKVCR EKLNFLYLIY SYICDTAGLH
TLVKDIVTWI QSSPLIEYWI YSYMLYRYFI DVFEGLSFLD PSTDMSARNP LLKRFYDAIK
PANISALTPT DSCLYIKTLY DKISSGASPS STVTKEIGKE VVSTTKHIFF YAFLQMHAHT
QLQDSAMYCR SRGICLKGDL SFGTSPVGVD SWVYPEYFEK SRVVGAPPDA FTPMGQNWGY
PAYNWRKMEE IDGYQWMQRR LKHAELFFDC VRLDHILGLF RTWELPLTAG KNNGSLGQFV
PAAPLHWDWI FEECYDPNSS ISWCRSKSDI RTRLTQPLLK RDLAHKLAGH AAGDLACSTL
VEFGVLSYDK RTDSYVIELQ EQKACALLDS LLLNEDIALE LHSALMETYR KLLGNVCLLN
DVSNPDAFCH PVFTNRHVSS EAVSLTSLEH IGLRDKIRHW SYEYFTTWHN DEWTRSGTKH
LRLIKESTNM MICGEDLGYL HPCIRRVMAD LGIIGLRVQR MTHEGYPGHF YRCDDESVYS
YLTVAAPSTH DTYPLRAWWE HNRSAACAFW RENLGRAGDS DWQVSRSLSE FDCRAILRQN
LHSRSIICCL MLQDIFGACD KYRYNGDTKD EIINMPGASE WQWKYRIHIS LEELHNSDLV
GIIGDEICNS GRILQ
//
