ID G8TAD9_NIAKG Unreviewed; 1104 AA.
AC G8TAD9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
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 OrderedLocusNames=Niako_0703 {ECO:0000313|EMBL:AEV97086.1};
OS Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS GR20-10).
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=700598 {ECO:0000313|EMBL:AEV97086.1, ECO:0000313|Proteomes:UP000005438};
RN [1] {ECO:0000313|EMBL:AEV97086.1, ECO:0000313|Proteomes:UP000005438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10
RC {ECO:0000313|Proteomes:UP000005438};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Davenport K.,
RA Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Niastella koreensis GR20-10.";
RL Submitted (DEC-2011) 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}.
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DR EMBL; CP003178; AEV97086.1; -; Genomic_DNA.
DR RefSeq; WP_014217000.1; NC_016609.1.
DR AlphaFoldDB; G8TAD9; -.
DR STRING; 700598.Niako_0703; -.
DR KEGG; nko:Niako_0703; -.
DR PATRIC; fig|700598.3.peg.719; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG3281; Bacteria.
DR HOGENOM; CLU_007635_1_0_10; -.
DR OMA; QEDRFPI; -.
DR OrthoDB; 9806009at2; -.
DR Proteomes; UP000005438; Chromosome.
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; IPR040999; Mak_N_cap.
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; PF18085; Mak_N_cap; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AEV97086.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 22..416
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1104 AA; 128825 MW; 717C276C8ECFF888 CRC64;
MEPTKQAFNE KLHWYKDAII YELHIKAFCD SNGDGIGDFG GLMQKLDYLQ ELGVNAIWLL
PFYPSPLRDD GYDIADYYNI NQSYGNITQL KTLLHEAHQR NLKIITELVI NHTSDQHPWF
QRARSAPKGS PERDYYVWTD DPSQYKDVRI IFQDFEASNW TWDPLAEQYY WHRFFHHQPD
LNYDNPLVQQ EVFNMIDFWC NMGVDGFRLD AVPYLYEREG TNGENLPETH AFLKRLRAHV
DAKFPGTVLL AEANMWPEDS ASYFGDGDEC HMNYHFPVMP RMFMALQMED RYPITDIFDQ
TPAIPPTCQW AIFLRNHDEL TLEMVTDEER DYMYKVYAKD PKARINLGIR HRLAPLMENN
REKIELLNTL LFALPGTPVI YYGDEIGMGD NYYLGDRDGV RTPMQWSPDR NAGFSHANPH
QLYLPLILDP EYHYESVNVE MQRRNTSSLF WFMKRMINMR KKHKAFGRGD LTFLNVDNPK
VLAFLRKYED ETLLIVVNLS KFAQVAEVPL EGYKGFALIE LMSRNKFPAI GKAETYFFTL
APHTCLWFSL EKAHPDFDEK KSIPLIQINE FKDIVNKDYQ AELENDILPA YLKQSRWFTG
RARAIHNVEI IQQGNVPSSP EASLLLVEVT YESGLPELYR LIVTFVQNAV AKKLTDSFPH
SVIAHMHVKG QEGILCDALY VTTFQQWLFK NLLQNQTMVF KENIQIKFYN NGALSTYVAQ
HDDIKPKIFE GNRYQIAITY DNSFFLTIYR RVDYYINPDA EITHFLSEYA KFKYVPPFLG
AIEWMTDKGT ITTGMLQVMI ENHGNGYSYM QERVYNYIER ILAMKQDSLP SFESKGNLAD
PVPFEQLSPE LKDLLGSRAA EQARLIGMRT GEMHLALASG THLKDFRPEE FSLHYQRSLY
SAMVSLVREV FQNLKRNISR LPGDLQPEAE ELLKHRDEVL KVFKKIYDKK LDVLKIRIHG
FYNLSQILFT GKDIAIKGYG GDPLRPYSER RLKRSPLIDV ATMLRSFHNV VFEGFHANHH
ILKDNMPKYV PFLRLWAHYM GGFFMKAYLD TVKGSKFVPP DNADFRVMLQ TYLLEKSLLE
LNHSLNDGLH SIIMPMRTIR MIIK
//