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
//
