ID A0A0C1R4T1_9CYAN Unreviewed; 1120 AA.
AC A0A0C1R4T1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00012619};
DE EC=5.4.99.16 {ECO:0000256|ARBA:ARBA00012619};
DE AltName: Full=Maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00031378};
GN Name=treS {ECO:0000313|EMBL:KAF3886818.1};
GN ORFNames=DA73_0220180 {ECO:0000313|EMBL:KIE10803.1}, DA73_0400015995
GN {ECO:0000313|EMBL:KAF3886818.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE10803.1};
RN [1] {ECO:0000313|EMBL:KIE10803.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE10803.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
RN [2] {ECO:0000313|EMBL:KAF3886818.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3886818.1};
RA Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA Tripathy S.;
RT "Improved Assembly of Tolypothrix boutellei genome.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001595};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC subfamily. {ECO:0000256|ARBA:ARBA00005496}.
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:KIE10803.1}.
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DR EMBL; JHEG04000001; KAF3886818.1; -; Genomic_DNA.
DR EMBL; JHEG02000048; KIE10803.1; -; Genomic_DNA.
DR RefSeq; WP_038099778.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1R4T1; -.
DR STRING; 1479485.DA73_0220180; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000029738; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11334; AmyAc_TreS; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR032091; Malt_amylase_C.
DR InterPro; IPR045857; O16G_dom_2.
DR InterPro; IPR012810; TreS/a-amylase_N.
DR NCBIfam; TIGR02456; treS_nterm; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF16657; Malt_amylase_C; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KAF3886818.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029738};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 20..414
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1120 AA; 128671 MW; 81F7BFF206F14F6B CRC64;
MQNLLLKDDP LWFKSAIIYE VPVRAFADSN GDGIGDFRGL TEKLDYLQDL GVTALWVLPF
FPSPLRDDGY DIADYTNVNP IYGTLEDFKE FLEAAHSRDI RVIIELIVNH TSDQHPWFQR
ARRAPKGSKE RDFYVWNDNP EKYKEARIIF KDFETSNWAW DPIAKAYYWH RFYSHQPDLN
YDNPAVRQAV FDVLDFWLGM GVDGLRLDAV PYLYEREGTN CENLFETHAF LKELRAHIDS
KFPNRMLLAE ANQWPEDAAQ YYGSGDECQM NFHFPLMPRL FMALRMEDNF PIIDILNQTP
SIPDNCQWAL FLRNHDELTL EMVTDEDRDY MYRVYAQDPV MRVNLGIRRR LAPLLGNDRR
QIELLNSLLL SLPGTPVLYY GDEIGMGDNV YVGDRNGVRT PMQWSSDRNA GFSRTNPQKL
YLPVIVESEY HYEAVNVEAQ RSNPNSLWYW TKRLLATRKR FQAFGLGTFE LLHPRNRKVL
AFTRNYDGQT ILVVANLSRF VQTVELDLSP FKGLVPMEIF GHTEFPAIGD SCYFLSLSPY
GFYWFALSPK ATLTQPPRPQ ADLTTLVVTG QWQNVFTQRE AKATLESILQ GYLYTCNWFT
SKTLTVQSTQ INETVLISYK DTEAKMVWLR VDYIQGDAET YLLVFAYAEG EQARQILADN
PQAVVARLEV QKIGVELETP PSGILFDATA DKNFLSLLVD AIAQNRSYKG MAGELGATAT
DLLPQLRGDE AYLDPTILQG EFQNTYVVYG NRLFLKIFRK LEEGMHPDLE LRRFLGEKKR
ITHFAPIAGA LEYRSVNRTG LLPAQPMTVG ILQEYIQDTR NGWDYTLDSL QDYFDLAIAR
QVEVTEVPIP SNSPIELLSL EIPELAKETI GSYLASAQLL GQCTAELHIA LSCDSENSDF
APEPFSSFYQ RSIYQYARNL TGQVFLLLED KLHSLPSETQ KLAHAALNYQ QDILERYQLI
LNQKITAMRS RYHGDYNLKR VLYTGKDFII HDFEGSEGRS LSERRMKRSP LRDVAGMLLS
FHYAAQIGLR NEIESGMVRP EALPLMEAWS RFWYVWVSTA FLNSYLVTAG QDTFLPSTTT
ELQVLLDAFV LEKGIFALGS ELSDRSDKVN IPLQLILHLF
//
