ID I2AKZ8_9MYCO Unreviewed; 590 AA.
AC I2AKZ8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
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 ORFNames=W7S_25115 {ECO:0000313|EMBL:AFJ37972.1};
OS Mycobacterium sp. MOTT36Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1168287 {ECO:0000313|EMBL:AFJ37972.1, ECO:0000313|Proteomes:UP000002868};
RN [1] {ECO:0000313|EMBL:AFJ37972.1, ECO:0000313|Proteomes:UP000002868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOTT36Y {ECO:0000313|EMBL:AFJ37972.1,
RC ECO:0000313|Proteomes:UP000002868};
RX PubMed=22815454; DOI=10.1128/JB.00752-12;
RA Kim B.J., Choi B.S., Choi I.Y., Lee J.H., Chun J., Hong S.H., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare clinical strain
RT MOTT-36Y, belonging to the INT5 genotype.";
RL J. Bacteriol. 194:4141-4142(2012).
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; CP003491; AFJ37972.1; -; Genomic_DNA.
DR RefSeq; WP_008262145.1; NC_017904.1.
DR AlphaFoldDB; I2AKZ8; -.
DR GeneID; 77299531; -.
DR KEGG; mmm:W7S_25115; -.
DR PATRIC; fig|1168287.3.peg.5105; -.
DR HOGENOM; CLU_006462_2_1_11; -.
DR Proteomes; UP000002868; 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; 3.20.20.80; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 51..453
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 67520 MW; D883092090BBCEC4 CRC64;
MNDAKEAVEH HPEGGSHVQD GVVEHPDAED FNNAAALPTD PTWFKHAVFY EVLVRAFFDA
NADGAGDLRG LLGQLDYLQW LGIDCIWLPP FYDSPLRDGG YDIRDFYKVL PEFGTVEDFV
ALLNAAHERG IRVITDLVMN HTSDSHPWFQ ESRHDPDGPY GDYYVWSDTS ERYTDARIIF
IDTEESNWTF DPVRKQFYWH RFFSHQPDLN YENPAVQEAM IDVLRFWLGL GIDGFRLDAV
PYLFEREGTN CENLPETHAF LKRVRKVVDD EFPGRVLLAE ANQWPADVVE YFGDPSTGGD
ECHMAFHFPL MPRIFMAVRR ESRFPISEIL AQTPEIPDMA QWGIFLRNHD ELTLEMVTDE
ERDYMYSEYA KDPRMKANVG IRRRLAPLLD NDRNQIELFT ALLLSLPGSP VLYYGDEIGM
GDVIWLGDRD GVRTPMQWTP DRNAGFSKAN PGRLYLPPSQ DSVYGYQAVN VEAQRDTSTS
LLNFTRTMLA VRRRHEAFAI GSFEELGGSN PSVLAFLRQV SGDGDTVLCV NNLSRFPQPI
ELNLQHWSGR TPVELTGQVE FPRIGHLPYL LTLPGHGFYW FRLSGCEEDA
//