ID   Q3J3M7_CERS4            Unreviewed;      1102 AA.
AC   Q3J3M7;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=RSP_2446 {ECO:0000313|EMBL:ABA78607.1};
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=272943 {ECO:0000313|EMBL:ABA78607.1, ECO:0000313|Proteomes:UP000002703};
RN   [1] {ECO:0000313|Proteomes:UP000002703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC
RC   12203 / NCIMB 8253 / ATH 2.4.1. {ECO:0000313|Proteomes:UP000002703};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) 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}.
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DR   EMBL; CP000143; ABA78607.1; -; Genomic_DNA.
DR   RefSeq; WP_011337497.1; NZ_CP030271.1.
DR   RefSeq; YP_352508.1; NC_007493.2.
DR   AlphaFoldDB; Q3J3M7; -.
DR   STRING; 272943.RSP_2446; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABA78607; ABA78607; RSP_2446.
DR   KEGG; rsp:RSP_2446; -.
DR   PATRIC; fig|272943.9.peg.1365; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   OrthoDB; 9805159at2; -.
DR   PhylomeDB; Q3J3M7; -.
DR   Proteomes; UP000002703; Chromosome 1.
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, ECO:0000313|EMBL:ABA78607.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002703}.
FT   DOMAIN          33..427
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1102 AA;  124131 MW;  FAA552E91F2942A8 CRC64;
     MNQNVSPSTV AVRRTDGIDR SQTDWYKDAI IYQLHIKAFQ DANGDGIGDF AGLMQRLDYV
     QALGVTAIWL LPFYPSPLRD DGYDISDYRS INPSYGAMRD FKLFVQEAHK RGLRVITELV
     INHTSDQHPW FQRARRAKKG SAARDWYVWS DTDQKFPETR IIFLDTEKSN WTWDPVAGAY
     YWHRFYSHQP DLNFDNPRVL EEVLKIMRMW LEMGVDGLRL DAIPYLVERE GTNNENLPET
     HDVLKKIRAN LDQHFPDRML LAEANQWPED TRPYFGEGDE CHMGFHFPLM PRMYMALAQA
     DRHPITDIIR QTPEIPEGCQ WGIFLRNHDE LTLEMVTAEE RDYMWRFYAE DSRARINLGI
     RRRLAPLMKN DRRKIELLNQ MLMSMPGTPI VYYGDEIGMG DNYYLGDRDG VRTPMQWSAD
     RNGGFSRCNP QQLYLPTILD PVYGHQAINV EAQAADPSSL LNWTRRLIAV RKQHPAFGRG
     SMSLLYPRNR KVLAYVRSHE GTDILCVANL SDTAQAVELD LGRFRGAVPV ELTGRSEFPP
     VGDLPYMLTL PPYGFYWFIL SDQQALPSWH QPMPETLPDF ITLTTRDGRA ETALTGRETR
     QLEADVLPNW LPLQRWFGAK EEKISAVKLA VLGSLSADHA LVRLEADVGG EVQQYFLPAS
     ALWGEEQLRA GAPKLSFTLA KVRRGPQVGA LIDGAYDEQM AQAMLEALRD GRRLSGAGGE
     VVFEPGSGLA EIADPGEPRY LGAEQSNISI AFGDRLILKL YRRLRAGEQP DVEVARFLTE
     VAGYTHTPRY LGVVSLRPAE GEATVLAAAF AFVANMGDAW RGLFDALVRD LGEFGGWSTA
     EAPEVEKDGF SFPLTIPGLL GQRTAELHQA FATETDEAAF RMEPLTAQHL TGWAEGARRE
     AEAMLSVLER QRTHLPDEVL PLAEALLARR EDLLARLDRV TGFEPSGALT RIHGDYHLGQ
     VLLAQDDVAI IDFEGEPRRT LAERREKSSP LRDVAGMLRS FDYAAAAALA RHEESFGPAS
     ERAVERAEAW RQQAVADFLA AYEGASAGTA SLPSDPALKE ALLDLFLVQK AVYETSYELG
     SRPAWVGIPL RGLLELLDRK PA
//