ID A0A093VNB3_TALMA Unreviewed; 505 AA.
AC A0A093VNB3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000256|RuleBase:RU367111};
DE EC=3.2.1.55 {ECO:0000256|RuleBase:RU367111};
GN ORFNames=GQ26_0052550 {ECO:0000313|EMBL:KFX51474.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX51474.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX51474.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX51474.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC Evidence={ECO:0000256|ARBA:ARBA00001462,
CC ECO:0000256|RuleBase:RU367111};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834, ECO:0000256|RuleBase:RU367111}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU367111}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 54 family.
CC {ECO:0000256|ARBA:ARBA00006963, ECO:0000256|RuleBase:RU367111}.
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:KFX51474.1}.
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DR EMBL; JPOX01000005; KFX51474.1; -; Genomic_DNA.
DR EMBL; JPOX01000005; KFX51476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093VNB3; -.
DR eggNOG; ENOG502QS3Q; Eukaryota.
DR HOGENOM; CLU_029332_3_0_1; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR015289; A-L-arabinofuranosidase_B_cat.
DR InterPro; IPR038964; ABFB.
DR InterPro; IPR007934; AbfB_ABD.
DR InterPro; IPR036195; AbfB_ABD_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR PANTHER; PTHR39447; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR PANTHER; PTHR39447:SF2; ALPHA-L-ARABINOFURANOSIDASE B; 1.
DR Pfam; PF05270; AbfB; 1.
DR Pfam; PF09206; ArabFuran-catal; 1.
DR SUPFAM; SSF110221; AbfB domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU367111};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR638964-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|RuleBase:RU367111};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367111};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU367111};
KW Secreted {ECO:0000256|RuleBase:RU367111};
KW Signal {ECO:0000256|RuleBase:RU367111};
KW Xylan degradation {ECO:0000256|RuleBase:RU367111}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU367111"
FT CHAIN 26..505
FT /note="Alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|RuleBase:RU367111"
FT /id="PRO_5009749805"
FT DOMAIN 27..341
FT /note="Alpha-L-arabinofuranosidase B catalytic"
FT /evidence="ECO:0000259|Pfam:PF09206"
FT DOMAIN 359..500
FT /note="Alpha-L-arabinofuranosidase B arabinose-binding"
FT /evidence="ECO:0000259|Pfam:PF05270"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT ACT_SITE 304
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-1"
FT DISULFID 28..38
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 88..93
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 184..185
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
FT DISULFID 408..446
FT /evidence="ECO:0000256|PIRSR:PIRSR638964-3"
SQ SEQUENCE 505 AA; 52413 MW; 09B7D9A9CCE003EB CRC64;
MMSSKQANRL NSMLALIFLI QSTLAGPCDI YSSGGTPCVA AHSTTRALYD SYTGVLYQIS
RGSDGATTDI SPLTAGDVAN ASAQDAFCAS TTCLITIIYD QSGQGNHLTQ APPGGAATGP
EANGYDYLAS AIGAPVMLNS DKAYGVFISP TNGYRVDDAT GIATGDEPEG LYAVLDGTHY
NTACCFDYGN AEVSNTDTGN GHMEAIYFGA DTRTGSGDGP GPWIMADLEN GLFSGYTAGN
NNADITMSSR FVTATLKGEA DQWAIRGGDA TSGSLTTLYS GIRPANGYNP MSKEGAIILG
IGGDNSDGAQ GTFYEGVMTS GYPSDDVENE VQANIVAAGY AITSLISGPG LTVGSSVSLR
ATTACCTTNY VSHSGSTVEL QVVNSSSTTA LQQQASWTVC TGLGNSGCYS FESVDTPGSY
IRHSNNQLQL NANDGTKLFS EDATFCPQAG LNSQGNSIRS WSYPGRFWRH YGGVLYIAAN
GGPNTFDSTT LYNDDVSFVI STGFA
//
