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Database: UniProt
Entry: I4ERV6_9ACTN
LinkDB: I4ERV6_9ACTN
Original site: I4ERV6_9ACTN 
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
//
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