XYNA_TALFU
ID XYNA_TALFU Reviewed; 529 AA.
AC Q8WZJ4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=1,4-beta-D-glucan cellobiohydrolase xynA;
DE EC=3.2.1.91;
DE AltName: Full=Beta-glucancellobiohydrolase xynA;
DE AltName: Full=Exocellobiohydrolase xynA;
DE AltName: Full=Exoglucanase xynA;
DE Flags: Precursor;
GN Name=xynA;
OS Talaromyces funiculosus (Fruitlet core rot fungus) (Penicillium
OS funiculosum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=28572;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 118-129 AND 274-288,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=IMI 134756;
RX PubMed=12664153; DOI=10.1007/s00253-002-1184-4;
RA Alcocer M.J., Furniss C.S.M., Kroon P.A., Campbell M., Archer D.B.;
RT "Comparison of modular and non-modular xylanases as carrier proteins for
RT the efficient secretion of heterologous proteins from Penicillium
RT funiculosum.";
RL Appl. Microbiol. Biotechnol. 60:726-732(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=22776993; DOI=10.1007/s10295-012-1166-1;
RA Texier H., Dumon C., Neugnot-Roux V., Maestracci M., O'Donohue M.J.;
RT "Redefining XynA from Penicillium funiculosum IMI 378536 as a GH7
RT cellobiohydrolase.";
RL J. Ind. Microbiol. Biotechnol. 39:1569-1576(2012).
CC -!- FUNCTION: The biological conversion of cellulose to glucose generally
CC requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC cut the disaccharide cellobiose from the non-reducing end of the
CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC cellobiose and other short cello-oligosaccharides to glucose.
CC {ECO:0000269|PubMed:22776993}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC and cellotetraose, releasing cellobiose from the non-reducing ends of
CC the chains.; EC=3.2.1.91; Evidence={ECO:0000269|PubMed:22776993};
CC -!- ACTIVITY REGULATION: Cellobiose inhibits xynA at high concentrations.
CC {ECO:0000269|PubMed:22776993}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.238 mM for 4-nitrophenyl-beta-D-cellobioside
CC {ECO:0000269|PubMed:22776993};
CC KM=0.57 mM for 4-nitrophenyl-beta-D-lactopyranoside
CC {ECO:0000269|PubMed:22776993};
CC pH dependence:
CC Optimum pH is 3.0-4.5. {ECO:0000269|PubMed:22776993};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:22776993};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12664153}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally identified as a 1,4-beta-D-xylan
CC xylanohydrolase (PubMed:12664153). However, further sequence
CC comparisons and enzymatic studies showed that xynA was principally an
CC 1,4-beta-D-glucan cellobiohydrolase (PubMed:22776993).
CC {ECO:0000305|PubMed:12664153, ECO:0000305|PubMed:22776993}.
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DR EMBL; AJ312295; CAC85737.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8WZJ4; -.
DR SMR; Q8WZJ4; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH7; Glycoside Hydrolase Family 7.
DR CLAE; CBH7A_PENFN; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd07999; GH7_CBH_EG; 1.
DR Gene3D; 2.70.100.10; -; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001722; Glyco_hydro_7.
DR InterPro; IPR037019; Glyco_hydro_7_sf.
DR PANTHER; PTHR33753; PTHR33753; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..529
FT /note="1,4-beta-D-glucan cellobiohydrolase xynA"
FT /id="PRO_5000067499"
FT DOMAIN 493..529
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 26..456
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 413..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..493
FT /note="Thr-rich linker"
FT /evidence="ECO:0000250"
FT REGION 460..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 234
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 239
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 501..518
FT /evidence="ECO:0000250"
FT DISULFID 512..528
FT /evidence="ECO:0000250"
SQ SEQUENCE 529 AA; 55048 MW; 95232F53577B6416 CRC64;
MSALNSFNMY KSALILGSLL ATAGAQQIGT YTAETHPSLS WSTCKSGGSC TTNSGAITLD
ANWRWVHGVN TSTNCYTGNT WNTAICDTDA SCAQDCALDG ADYSGTYGIT TSGNSLRLNF
VTGSNVGSRT YLMADNTHYQ IFDLLNQEFT FTVDVSNLPC GLNGALYFVT MDADGGVSKY
PNNKAGAQYG VGYCDSQCPR DLKFIAGQAN VEGWTPSTNN SNTGIGNHGS CCAELDIWEA
NSISEALTPH PCDTPGLTVC TADDCGGTYS SNRYAGTCDP DGCDFNPYRL GVTDFYGSGK
TVDTTKPFTV VTQFVTDDGT SSGSLSEIRR YYVQNGVVIP QPSSKISGIS GNVINSDFCA
AELSAFGETA SFTNHGGLKN MGSALEAGMV LVMSLWDDYS VNMLWLDSTY PANETGTPGA
ARGSCPTTSG NPKTVESQSG SSYVVFSDIK VGPFNSTFSG GTSTGGSTTT TASGTTSTKA
STTSTSSTST GTGVAAHWGQ CGGQGWTGPT TCASGTTCTV VNPYYSQCL
