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Database: UniProt
Entry: A0A068REB3_9FUNG
LinkDB: A0A068REB3_9FUNG
Original site: A0A068REB3_9FUNG 
ID   A0A068REB3_9FUNG        Unreviewed;       313 AA.
AC   A0A068REB3;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Arabinan endo-1,5-alpha-L-arabinosidase {ECO:0000256|ARBA:ARBA00012586, ECO:0000256|PIRNR:PIRNR026534};
DE            EC=3.2.1.99 {ECO:0000256|ARBA:ARBA00012586, ECO:0000256|PIRNR:PIRNR026534};
GN   ORFNames=LCOR_00258.1 {ECO:0000313|EMBL:CDH48478.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH48478.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH48478.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in
CC         (1->5)-arabinans.; EC=3.2.1.99;
CC         Evidence={ECO:0000256|ARBA:ARBA00000375,
CC         ECO:0000256|PIRNR:PIRNR026534};
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834, ECO:0000256|PIRNR:PIRNR026534}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|PIRNR:PIRNR026534}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDH48478.1}.
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DR   EMBL; CBTN010000001; CDH48478.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068REB3; -.
DR   STRING; 1263082.A0A068REB3; -.
DR   VEuPathDB; FungiDB:LCOR_00258.1; -.
DR   OrthoDB; 2418563at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000027586; Unassembled WGS sequence.
DR   GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd18829; GH43_BsArb43A-like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR   PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR026534};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR026534};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027586};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..313
FT                   /note="Arabinan endo-1,5-alpha-L-arabinosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001652499"
FT   ACT_SITE        36
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        206
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            152
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   313 AA;  33847 MW;  332667BA7AE043F5 CRC64;
     MLFGKISTGI LFASSLLVSQ VYGDFWNLSG DIGCHDPTII KEDSTWFAFC TGDGIQAKYS
     NDKTTWESAA QIFLSAPSWW ASAASGHSGL DVWAPDAKVF NNRVYLYYAI SSFGSQNSAI
     GLASADSIKA GSWRDDGLVL KTTSSNDYNA IDPELVIDND GKPWLAFGSF WSGLKITELD
     PATMKPYQNA KIYSIAANPN DSNAIEAASI VYHDGYYYLF ASIDKCCSGV DSTYKIVVSR
     SKSITGPYLD KNGVDAMQSA GTIFDAGNDK WIGPGGQDVN DGVIARHAYD AEDNGAPKLL
     INDLNWSGGW PTY
//
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