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Database: UniProt
Entry: A3WWG0_9BRAD
LinkDB: A3WWG0_9BRAD
Original site: A3WWG0_9BRAD 
ID   A3WWG0_9BRAD            Unreviewed;      1094 AA.
AC   A3WWG0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 67.
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=NB311A_12694 {ECO:0000313|EMBL:EAQ35681.1};
OS   Nitrobacter sp. Nb-311A.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Nitrobacter.
OX   NCBI_TaxID=314253 {ECO:0000313|EMBL:EAQ35681.1, ECO:0000313|Proteomes:UP000003725};
RN   [1] {ECO:0000313|EMBL:EAQ35681.1, ECO:0000313|Proteomes:UP000003725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nb-311A {ECO:0000313|EMBL:EAQ35681.1,
RC   ECO:0000313|Proteomes:UP000003725};
RA   Waterbury J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (JAN-2006) 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:EAQ35681.1}.
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DR   EMBL; AAMY01000009; EAQ35681.1; -; Genomic_DNA.
DR   RefSeq; WP_009797380.1; NZ_AAMY01000009.1.
DR   AlphaFoldDB; A3WWG0; -.
DR   STRING; 314253.NB311A_12694; -.
DR   HOGENOM; CLU_007635_1_2_5; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000003725; Unassembled WGS sequence.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR012810; TreS/a-amylase_N.
DR   InterPro; IPR012811; TreS_maltokin_C_dom.
DR   NCBIfam; TIGR02457; TreS_Cterm; 1.
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.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003725}.
FT   DOMAIN          27..426
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1094 AA;  125130 MW;  5FAFC5FFA08ED594 CRC64;
     MNKMSHIDAD RYVQTDDLWY KDAIIYQLHV KAFADSNNDG IGDFVGLTNK LDYLQELGVT
     ALWLLPFYPS PGRDDGYDIA DYGSINPDFG TMKDFRRFIS EAKRRGLRVI TELVINHTSD
     QHRWFKRAQR SPQGSSARNW YVWSNTDKKY QGTRIIFTDT EKSNWAWDAE ANAYYWHRFF
     SHQPDLNFDN PRVVRAVVQV MKRWLDTGVD GFRLDAIPYL CEREGTNNEN LPETHAVIKH
     IRAELDAYAK GKVLLAEANQ WPEDVQFYFG DGDECHMAYH FPLMPRIYMA IAQEDRFPIT
     DILRQTPDIP DSCQWAMFLR NHDELTLEMV TDIERDYLWS TYAADPRARI NLGIRRRLAP
     LMDNDRRKIE LMNSLLMSLP GTPIIYYGDE IGMGDNIYLG DRNGVRTPMQ WTPDRNGGFS
     RCDPARLYAP PVMDAVYGYE SVNVEAQSRS LSSLLSWMKK LISVRKSSHA FGRGTMSFAR
     SSNRSVLAYV RQYNDEVVLC VANLSRSAQA SELDLSHWKG RSPLEMLGRT TFPDIGELPY
     LITLAPYGFY WFRLNEKPSS PNVATVIIPD YETLVVPVGA TWMSLARTRL IFERDVLPSY
     LARSRWFPER SAGSIIARVP AAVPLMEDQV SRPWLVIFDV SHRGKSGRYA MPIRIRWDRL
     DRRNYDVKNI AAVRQGSREG TLIDAAYESD LIAGIIEGLR RRATFEEGNL RLAHVPTERM
     ASIAEEPIEN VRAVQTEQSN STALVDQKFV VKLYRKIENG INPEVEVGRF LTDVAGFANT
     PALLGSVELT GPDVETAIAI VHAFVGNQGD AWTVTSAALD RFVDEQRLVG AVYSAPALEE
     KAAYQRYMVQ TGKRVAEMHM ALASRDDIEN FRPEPVTASD VAHLIDRLMT HAEQTFDRLA
     QTKLLESDQL LVEEIQSLRP ALHSLLTRLL PSSIQMHNIR HHGDLHLGQV LVVRDDVFII
     DFEGEPRRSL SERRMKAPAA RDVAGLIRSI DYSVTSAQER VLKTEADDDG RLAEALSAWR
     DEATQTFLAS YREAMSDFRL WPQDKNDEDG MLQFFLLEKA IYEIDYELAH RPDWLRVALD
     GALRVLHNRK RDRA
//
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