ID   G0JKR3_9PROT            Unreviewed;      1138 AA.
AC   G0JKR3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
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=Acife_0606 {ECO:0000313|EMBL:AEM46809.1};
OS   Acidithiobacillus ferrivorans SS3.
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=743299 {ECO:0000313|EMBL:AEM46809.1, ECO:0000313|Proteomes:UP000009220};
RN   [1] {ECO:0000313|EMBL:AEM46809.1, ECO:0000313|Proteomes:UP000009220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS3 {ECO:0000313|EMBL:AEM46809.1,
RC   ECO:0000313|Proteomes:UP000009220};
RX   PubMed=21705598; DOI=10.1128/JB.05373-11;
RA   Liljeqvist M., Valdes J., Holmes D.S., Dopson M.;
RT   "Draft genome of the psychrotolerant acidophile Acidithiobacillus
RT   ferrivorans SS3.";
RL   J. Bacteriol. 193:4304-4305(2011).
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; CP002985; AEM46809.1; -; Genomic_DNA.
DR   RefSeq; WP_014028078.1; NC_015942.1.
DR   AlphaFoldDB; G0JKR3; -.
DR   STRING; 743299.Acife_0606; -.
DR   KEGG; afi:Acife_0606; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_0_1_6; -.
DR   Proteomes; UP000009220; 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; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009220}.
FT   DOMAIN          34..433
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1138 AA;  128957 MW;  99957983556531BA CRC64;
     MTAEKTEAGA APDTAAVASA GGDTLWYKDA ILYELHVRTF QDSNGDGIGD FPGLTSRLDY
     LQDLGVNTLW LLPFYPSPLR DDGYDISDYR GIHPDYGTLD DFRHFLHEAH RRGLKVITEL
     VINHSSDQHP WFQAARRAPP GSAKRNYYVW SDTDKKFPET RIIFSDSERS NWAWDDVAKA
     YYWHRFFSHQ PDLNHNNPQV VKAMIRVLRY WLDMGVDGLR LDAIPYLCVR AGTDNENLPE
     THAVIRQIRS AVDAHYRDRV LLAEANQWPE DVREYFGQGD ECQMAYHFPL MPRVYMSLAL
     EDRHPITDIL RQTPDIPENC QWAIFLRNHD ELTLEMVTRQ ERDYLYREYA ADPRMRLNLG
     IRRRLAPLLG NDRQKIKLLT WLLMSMPGSP IVYYGDEIGM GDNIYLGDRN GVRTPMQWSP
     DYNGGFSRAD PEQLYLPLLM DPVYGYQAVN VESQSRNASS LLHWTRKVIA VRKEHPAFGR
     GNIRFLRPGN RKMLAYLREY AGVSVLCVAN LARTAQAVEL GLEAYAGRTP VELMGKSAFP
     PIGQLPYLLT LPAYAFLAFA LAEDTTPPAW HEERLARPEL PALVLLEGWR TFLSLDGEAS
     DIRRALAART RRQLQEEVLT PYLRGKHWAA DDRETVPTVV VEIEDEWRAP GGQQGWLWMI
     IQIPGTDGEN RHYSLPLAIA WEDEQENLMD TFHTWILARV RQRERLGVLL DAFGDDAFCR
     TLVRSMDTGG EHPFAGGILA FEKSAAWDFS ESDLNTLQRP SLEQRHNNIL FGEQLYLKGY
     RHLQAGGDPE FEVGVFLTEV SPYTHMAPVL GRVEFRPAQG DALALALLRR YVENQGDAWT
     FSVEYLERTL TERMTAAVPG ADASPQRENG HALYRLRMAT LGRRVAELHR ALEQPGGDQA
     FDPEPFTAED LAQWVDHTAQ VAAKAAAALE EALPDLPEGL RQNAQDWLAA QARIPERLAT
     WRHLPLPATL TRIRCPGHLG LAQVLLVDED FILINLGGDP RLSPVQRRHK QSPLLDLAAM
     RLSLMAAALA ALRRLSARAG DDLPQLREWA RTWAKQSLDA FAQAYDEIAT GAAFYPADLS
     LREKLLELAL WERLLGDIPE LLEPLQEDIL GGTLRILLAA METASEQTPD AAIWAGLT
//