ID I0KBK1_9BACT Unreviewed; 748 AA.
AC I0KBK1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Malto-oligosyltrehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00015938};
DE EC=3.2.1.141 {ECO:0000256|ARBA:ARBA00012268};
DE AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00033284};
DE AltName: Full=Maltooligosyl trehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00032057};
GN Name=treZ {ECO:0000313|EMBL:CCH01504.1};
GN ORFNames=FAES_3497 {ECO:0000313|EMBL:CCH01504.1};
OS Fibrella aestuarina BUZ 2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrella.
OX NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCH01504.1, ECO:0000313|Proteomes:UP000011058};
RN [1] {ECO:0000313|EMBL:CCH01504.1, ECO:0000313|Proteomes:UP000011058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 2T {ECO:0000313|Proteomes:UP000011058};
RX PubMed=22689241; DOI=10.1128/JB.00550-12;
RA Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine
RT Bacterium.";
RL J. Bacteriol. 194:3555-3555(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-
CC [(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-
CC alpha-D-glucan.; EC=3.2.1.141;
CC Evidence={ECO:0000256|ARBA:ARBA00034013};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005199}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; HE796683; CCH01504.1; -; Genomic_DNA.
DR AlphaFoldDB; I0KBK1; -.
DR STRING; 1166018.FAES_3497; -.
DR KEGG; fae:FAES_3497; -.
DR PATRIC; fig|1166018.3.peg.5273; -.
DR eggNOG; COG0296; Bacteria.
DR eggNOG; COG3147; Bacteria.
DR HOGENOM; CLU_020726_2_0_10; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000011058; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:InterPro.
DR GO; GO:0033942; F:4-alpha-D-(1->4)-alpha-D-glucanotrehalose trehalohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd11325; AmyAc_GTHase; 1.
DR Gene3D; 1.10.10.760; E-set domains of sugar-utilizing enzymes; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR037439; Branching_enzy.
DR InterPro; IPR022567; DUF3459.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR012768; Trehalose_TreZ.
DR InterPro; IPR044901; Trehalose_TreZ_E-set_sf.
DR NCBIfam; TIGR02402; trehalose_TreZ; 1.
DR PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF11; MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF11941; DUF3459; 1.
DR PIRSF; PIRSF000463; GlgB; 4.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CCH01504.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCH01504.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011058}.
FT DOMAIN 232..576
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 108..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 85028 MW; 4ECBE5E7EA9EF769 CRC64;
MAPAGGRTRP RRKTLSTMRF TDFTQPAPYR TTDWPRSLQV SHRQLGVTFP VPGQANVLVW
APLADDVALW LPAEAALLPL TKDLFGYWQL TTDQLAPGDL YAFVLNGQHP AESDSPAPDP
TDRDPAERSP AERSPTERSP TERSPTERSP TERSPTERSP TERSPTERSP TERSPTERSP
TERSPIPMLP DPASLSQPEG VHGLSRAVDT GTFPWEDTGW VNPPLAQYLL YELHTGTFTP
EGTFAGIEEK LDYLKALGVN AIEIMPIAEF PGDRNWGYDG VNLFAAHHAY GGATALQHLV
DACHFRGIAV VLDVVYNHFG PEGNYLSQFG PYLTDQYNTP WGKAVNYDDA WCDGVRRYVI
ENALMWLRDF HVDALRLDAV HAIKDFSPIH ILRELRQRVD ELSAQTGRTY YLIVESDLND
PRVINPLTEH GYGMDAQWVD EFHHALRVSV GEEPAGYYAD YERVYHLSKS YIDAYAYDGQ
FSQVRQKRFG LKVERHPGHQ FIVFSQNHDQ VGNRKGGERS CHLYSFEMLK LMAGAVLVSP
FIPMLFMGEE WAETNPFFYF VHHSDPALIA SVRAGRQAEF AAFYEDGNMP DPQRKQTFRQ
TKLQWHLPTE QPHQTLLRYY QTLITLRKQL PALYNLNRQT LRVFPDEEAH TLVLHRWHQD
QHLLCLMNFT TETRTVQLPD LPGDWTKLLD SADQAWLGPE GDSPTPDQCT GNASVYLHPE
SIVLYAQGHE SYRVTLPPPI PERLFIPH
//
