ID K5WIH8_PHACS Unreviewed; 496 AA.
AC K5WIH8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=glucan endo-1,6-beta-glucosidase {ECO:0000256|ARBA:ARBA00038935};
DE EC=3.2.1.75 {ECO:0000256|ARBA:ARBA00038935};
DE AltName: Full=Beta-1,6-glucanase B {ECO:0000256|ARBA:ARBA00042025};
DE AltName: Full=Endo-1,6-beta-D-glucanase B {ECO:0000256|ARBA:ARBA00041472};
DE AltName: Full=Endo-1,6-beta-glucanase B {ECO:0000256|ARBA:ARBA00043257};
GN ORFNames=PHACADRAFT_166617 {ECO:0000313|EMBL:EKM50047.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM50047.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM50047.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM50047.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
CC -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC the main structural component of the cell wall. Acts on lutean,
CC pustulan and 1,6-oligo-beta-D-glucosides.
CC {ECO:0000256|ARBA:ARBA00037628}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-
CC glucans.; EC=3.2.1.75; Evidence={ECO:0000256|ARBA:ARBA00036633};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR EMBL; JH930479; EKM50047.1; -; Genomic_DNA.
DR RefSeq; XP_007401241.1; XM_007401179.1.
DR AlphaFoldDB; K5WIH8; -.
DR GeneID; 18909350; -.
DR KEGG; pco:PHACADRAFT_166617; -.
DR HOGENOM; CLU_004624_7_1_1; -.
DR InParanoid; K5WIH8; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR PANTHER; PTHR31297:SF39; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:EKM50047.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008370}.
FT DOMAIN 57..403
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 439..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 54554 MW; F7852BCD92AFE444 CRC64;
MPDKIYGVNL GSWLVLESWM LPAEWLAMGG QSCSDCSQCI ATEFAFAQAY PDTVDQKFEQ
HWESWFTQDD VDQIAAAGIN TVRIPLGYWI IEPLVNRTSE FYPRGGIKQL QRGLSQLQAA
GIVAILDHHA LPGVQTAGQM FTGHCTNDVE FYTEYNYHRA LIWTAVMTAL SHLDPNFGSV
FAIEAVNEPI MDATQTPGYG TFQANFVKVV RAVELILGIP VPGIQLDVPV NTSNFTYALG
DVTNATTLTE IFNDEVKSAL EDAIPILAEI AIELAIPTIF NFELEEAPCH SNPEPLVTNF
MDVNWQFNNP PNPAAAAIGP QGYDNHLYYS FGGVADPNPD AYLTSICNLQ RVQNDAAVGD
SPLWFGEWGL PTQFNATDDF LFKWADAQKL AYSQGAGWIF WNFKVEISQL AGDLARQWSY
LEGLRLGYLT QDPSQVHDSN VCDPYRNNGT STSTGTGTSA STSTSAGIST SASDSTPTSN
GTLVRKRHGH KRQRIH
//
