ID K9RAZ7_9CYAN Unreviewed; 1132 AA. AC K9RAZ7; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 27-MAR-2024, entry version 42. 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=Riv7116_2079 {ECO:0000313|EMBL:AFY54611.1}; OS Rivularia sp. PCC 7116. OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Rivulariaceae; OC Rivularia. OX NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY54611.1, ECO:0000313|Proteomes:UP000010380}; RN [1] {ECO:0000313|EMBL:AFY54611.1, ECO:0000313|Proteomes:UP000010380} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY54611.1, RC ECO:0000313|Proteomes:UP000010380}; RG US DOE Joint Genome Institute; RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M., RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N., RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A., RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.; RT "Finished chromosome of genome of Rivularia sp. PCC 7116."; RL Submitted (AUG-2012) 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP003549; AFY54611.1; -; Genomic_DNA. DR AlphaFoldDB; K9RAZ7; -. DR STRING; 373994.Riv7116_2079; -. DR KEGG; riv:Riv7116_2079; -. DR PATRIC; fig|373994.3.peg.2208; -. DR eggNOG; COG0366; Bacteria. DR eggNOG; COG3281; Bacteria. DR HOGENOM; CLU_007635_1_1_3; -. DR Proteomes; UP000010380; Chromosome. 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; IPR040999; Mak_N_cap. 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; 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 Calcium {ECO:0000256|ARBA:ARBA00022837}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AFY54611.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Reference proteome {ECO:0000313|Proteomes:UP000010380}; KW Transferase {ECO:0000256|ARBA:ARBA00022676}. FT DOMAIN 27..421 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" SQ SEQUENCE 1132 AA; 130169 MW; D456A1B4AA3A1670 CRC64; MRAVKKIMQN PLLKDDPLWF KDAVIYEVPV RAFADSDGDG IGDFGGLTEK LDYLQDLGVT AIWVLPFFPS PLRDDGYDIA DYTSVNPIYG NLEDFKNCLN AAHQRGIRVI IELIVNHTSD QHPWFQRARK APPGSPERDF YVWSDTPEKY EEARIIFKDF ETSNWTWDPV AKAYYWHRFY SHQPDLNFEN PQMQEALFEV VDFWLEMGVD GLRLDAVPYL YEREGTNCEN LEETHAFLKK IRKHMDEKFP NRMMLAEANQ WPEDAVEYYS GGDECHMNFH FPLMPRLFMG LQMEDSFPII DILQQTPPIP GNCQWALFLR NHDELTLEMV SDEDRDYMYR VYAQDQQARL NLGIRRRLAP LMGNNRRRIE VMNALLMSLP GTPVLYYGDE IAMGDNIYLG DRNGVRTPMQ WSADRNGGFS RCNPHKLYAP VIIDPEYHFE AVNVEAQREN RNSLWWWMKR LIATRGRFQA FGRGTFELLY PENRKVLAFT RTYNGEHILV VTNLSRFVQT VELDLAAFDG MIPVEIFGRT TFPAIDDAPY FMSLAPHAFY WFTLDVQTNI TCPVRPQNQI PTIVVSDNWR NIFTKSETKA ALEEMLPDYM CACSWFDSKS RVIQSSHVIE AIPISFRSLE AAIVLIQLDY TEGDPETYVL PLAYEPEGIN HERFSSYREE VVANIEIRSE KQTGVLFDAL ADKEFLNFPL EAIANKETYK GMAGQLVAES SKDFTELAGA GSNFGLKANL EAHLLRGEHN NTCVIYGDRL MCKLFRKVVG EGINPDLEVG QFLTHSSATT GLPGAENFAP VAGSLNYSRK GFETMTLGMV QKYIPDIRDG WVYSLDSLRD FFEQVQVTQI DAVADIDLPP SLLSAALETE IPEIAQEMIG SYLRNAQLLG ERTAEMHLAL VSDQEDPNFA PEAFTSFYQR SIYQYMRNQA GQVLLLLKKH LIQLPSDLQP VAQVVLNNRE MILARLKSIL NQKINAMRTR THGNLCLNEV LYTGKDFIII DFEGDQTRPL SERRMKRSPL RDVAGMLESF YYSSRIGLRN EKESGIILPD DQPLMEQWAQ FFYTWSSIAF LQSYLKAAKD APFIPSEPSE LQLLLDGFVL EKVIIELEHE LKNRPNWVEV PLYRILELLE TA //