ID K8EF37_CARML Unreviewed; 483 AA.
AC K8EF37;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 2.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Glycosyl hydrolase 1 family protein {ECO:0000313|EMBL:CCO10388.2};
DE EC=3.2.1.86 {ECO:0000313|EMBL:CCO10388.2};
GN Name=ascB {ECO:0000313|EMBL:CCO10388.2};
GN ORFNames=BN424_924 {ECO:0000313|EMBL:CCO10388.2};
OS Carnobacterium maltaromaticum LMA28.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1234679 {ECO:0000313|EMBL:CCO10388.2, ECO:0000313|Proteomes:UP000000212};
RN [1] {ECO:0000313|Proteomes:UP000000212}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LMA28 {ECO:0000313|Proteomes:UP000000212};
RX PubMed=23405327; DOI=10.1128/genomeA.00115-12;
RA Cailliez-Grimal C., Chaillou S., Anba-Mondoloni J., Loux V., Afzal M.I.,
RA Rahman A., Kergourlay G., Champomier-Verges M.C., Zagorec M., Dalgaard P.,
RA Leisner J.J., Prevost H., Revol-Junelles A.M., Borges F.;
RT "Complete Chromosome Sequence of Carnobacterium maltaromaticum LMA 28.";
RL Genome Announc. 1:0-0(2013).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR EMBL; HE999757; CCO10388.2; -; Genomic_DNA.
DR RefSeq; WP_015075790.1; NC_019425.2.
DR AlphaFoldDB; K8EF37; -.
DR STRING; 1234679.BN424_924; -.
DR KEGG; cml:BN424_924; -.
DR eggNOG; COG2723; Bacteria.
DR HOGENOM; CLU_001859_0_2_9; -.
DR OrthoDB; 1637462at2; -.
DR Proteomes; UP000000212; Chromosome.
DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353:SF348; 6-PHOSPHO-BETA-GLUCOSIDASE ASCB-RELATED; 1.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU004468};
KW Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:CCO10388.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000212}.
FT ACT_SITE 372
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 483 AA; 55347 MW; A086AE35DD8926C8 CRC64;
MTLDKNFLWG GATAANQAEG GVLEGGRKLS NIDVLPCGED RKKVALGELE MLDWQDGYYY
PAKEAIDMYH RYMEDIQLFA EMGFKVYRMS LSWSRIFPNG DDAEPNEEGL AFYESIFKEL
RKHQIEPLVT IAHFDVPIHL IKTYGGWKNR QLIEFYTRYA ETVLKRYKGL VKYWLTINEI
NILLHQPFVG GGIIFKEGEN QEEIKYQAAH HQLVASALAT KIAHEVDSRN QVGCMLAGGS
HYPYTCRPED YQEAINRDRE GYFFIDVQAR GKYPNYALKK LAREGLNIVM EVGDKEILAA
SPVDFVTFSY YCSRTVSAHS EDYEQSTGNI FASIKNKNLP STEWGWQIDP LGLRNSLNQL
YDRYQKPLFI VENGLGAIDI PDSNGYVEDE YRIDYLREHI QAFKDAVEID GVELLGYTTW
GCIDLVAAST GQMSKRYGFI YVDRDDEGNG SLARSKKKSF YWYQQVIETN GENLSSENLN
IEK
//