ID I4ERV6_9ACTN Unreviewed; 616 AA.
AC I4ERV6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Glycoside hydrolase family 43 (Modular protein) {ECO:0000313|EMBL:CCH86119.1};
GN OrderedLocusNames=MODMU_0662 {ECO:0000313|EMBL:CCH86119.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH86119.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH86119.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH86119.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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DR EMBL; FO203431; CCH86119.1; -; Genomic_DNA.
DR AlphaFoldDB; I4ERV6; -.
DR STRING; 477641.MODMU_0662; -.
DR KEGG; mmar:MODMU_0662; -.
DR PATRIC; fig|477641.3.peg.631; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_8_2_11; -.
DR OMA; KGWNTVT; -.
DR Proteomes; UP000006461; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd08999; GH43_ABN-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF5; ENDO-ARABINASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS51175; CBM6; 2.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCH86119.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..616
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003689018"
FT DOMAIN 349..473
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 492..616
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT ACT_SITE 54
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 241
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 181
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 616 AA; 64499 MW; 88CD3024991E30E5 CRC64;
MPSPTSHRRT AAAGALLALG LLAPAFTGTA QAAPPPSAGA QASIEPVIDA NFPDPDILVV
DGVYHAYATN NEGQNVQHQT STDLVHWTPQ PDAAPVLGDW VGPCSFAPGG ATDNCVWAPE
VSAVEGGYAL YYTARDESSQ LQCIGVATSA SPNGPFVPVG TEPLVCPTGQ DGTPALGGAI
DASTYREGGQ LYLLWKADGN CCAGKTAIIY LQPLSADGTT LTGPPTELIR RDQPFEGNVV
EAPTLVERNG TYYLFYSAND FAGGGYRTNY ATSTSLTGPY VKSRTELMTT DRFQGDVRGP
GGQDVVTNPD GSTSIVFHGW DPTYSYRAMY VSDLDWSATG VPSVAAASTR YQAEDGVVTN
ARVVADDTAS GLAKVGGLDA PDSSVTVQVY AEKAGPATLG IRYANGSVDA TGPVLATDTL
TVNGRSAGTV TFLHTTWGNW QLLEQQVKLQ KGWNTVTLTK ATAFAEIDAI DVYAADHGPA
PSAPPVVPAT AVRYEAEDGV VTHARVVDDP NASAGAKVGG LDFADSSVTL QVFADKAGPA
TLGIRFANGS DRGGYPVEST DTVTVNGQDA GVVTFWHTRW DNWTTVEHPV KLQKGWNTVT
LTRGTFYAEL DAVDVY
//