ID S7S595_GLOTA Unreviewed; 449 AA.
AC S7S595;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Galactan 1,3-beta-galactosidase {ECO:0000313|EMBL:EPQ61129.1};
GN ORFNames=GLOTRDRAFT_69366 {ECO:0000313|EMBL:EPQ61129.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ61129.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ61129.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ61129.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB469296; EPQ61129.1; -; Genomic_DNA.
DR RefSeq; XP_007861372.1; XM_007863181.1.
DR AlphaFoldDB; S7S595; -.
DR STRING; 670483.S7S595; -.
DR GeneID; 19307973; -.
DR KEGG; gtr:GLOTRDRAFT_69366; -.
DR eggNOG; ENOG502QW2A; Eukaryota.
DR HOGENOM; CLU_016116_1_1_1; -.
DR OMA; NDNYYST; -.
DR OrthoDB; 1937702at2759; -.
DR Proteomes; UP000030669; Unassembled WGS sequence.
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; cd04081; CBM35_galactosidase-like; 1.
DR CDD; cd18821; GH43_Pc3Gal43A-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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; PTHR22925:SF3; ARABINANASE_LEVANSUCRASE_INVERTASE; 1.
DR PANTHER; PTHR22925; GLYCOSYL HYDROLASE 43 FAMILY MEMBER; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51175; CBM6; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000030669};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..449
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004544709"
FT DOMAIN 324..446
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT SITE 158
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 449 AA; 48056 MW; E8CF4744D8E2D9AB CRC64;
MVALLLCSAL VFLLAALAHA ESVIVPGAAW TDTYGNVIQA HGGGILKVGN TYYWHGEDKT
TNSAEFRAVS CYSSTDLVNW ERNADALTPQ SGTMISTSNI VERPKVLYNS NNKEYVMWFH
SDSSNYGAAM VGVAIASSPC GPYSYKGSWQ PLGAQSRDMG VFQDDDGTAY LLYASDNNQN
FKISRMDSNY YNVTTQVNVL NGATLEAPGI VKRNGAYYLF ASHTSGWAPN PNKWFRASSL
SGNWTSQEDI APENTRTYYS QNNFDLPLGS NAIYMGDRWR PSLLGSSRYI WLPLSWSSGS
PQLVWVDVWS VNLAAGTYSA ASGTTYEAES GTLGGNATIL SDSSYSGGKA VGYLGNGGTV
TFDNVQGNGK GQWVSLYYGN GDSSYRNVTV SVNGGAAALV DQPDTGGGHV ILSVPVKLNL
KSGSNTITLG SGQSNYAGDL DKIIVYNVG
//
