ID A0A165CPZ3_EXIGL Unreviewed; 353 AA.
AC A0A165CPZ3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=mannan endo-1,4-beta-mannosidase {ECO:0000256|ARBA:ARBA00012706};
DE EC=3.2.1.78 {ECO:0000256|ARBA:ARBA00012706};
GN ORFNames=EXIGLDRAFT_729130 {ECO:0000313|EMBL:KZV82877.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV82877.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV82877.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV82877.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in
CC mannans, galactomannans and glucomannans.; EC=3.2.1.78;
CC Evidence={ECO:0000256|ARBA:ARBA00001678};
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; KV426299; KZV82877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165CPZ3; -.
DR STRING; 1314781.A0A165CPZ3; -.
DR InParanoid; A0A165CPZ3; -.
DR OrthoDB; 5489541at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProt.
DR GO; GO:0046355; P:mannan catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045053; MAN-like.
DR PANTHER; PTHR31451; MANNAN ENDO-1,4-BETA-MANNOSIDASE 7; 1.
DR PANTHER; PTHR31451:SF60; MANNAN ENDO-1,4-BETA-MANNOSIDASE 7; 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:KZV82877.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..353
FT /note="mannan endo-1,4-beta-mannosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007856107"
FT DOMAIN 40..303
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 353 AA; 38476 MW; F574D0F0E2DA3E03 CRC64;
MRAPALLAFA VAAATIPLAS AFASFAGANN YYAYALPSNE RSALLQSMNA AGMKVLRTFV
NGVGTGQKNS SNIAVNDLEP TTIRQYDDTI LNKIDQLMVE AHAWNIKLLI CIYDKNVLAA
RGPYKTKYTE SGFYTSAAAL DDYNQRITHM LNTHKNALLN NQPWSFLGAY IFGYSVMNEP
MINQGAGFFT QHLDWVCKVA AQIRANVGDK NQLIFTGGNS AGTSVQSFFF SSSCPAIDVV
EIHDYTDGYD SYMQNAINQA KASGKKLIIG EWGSLVGSGR TANLQSNMQK INGWGIPWLY
WEFITNPDPH QGEDYEINVN GGNDADYKTV KGFAQSAAAA TNGVFDWSGA LAL
//
