AXE1_COPC7
ID AXE1_COPC7 Reviewed; 374 AA.
AC A8PB24;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Acetylxylan esterase {ECO:0000303|PubMed:23180549};
DE Short=AXE {ECO:0000303|PubMed:23180549};
DE EC=3.1.1.72 {ECO:0000269|PubMed:23180549};
DE Flags: Precursor;
GN ORFNames=CC1G_12850;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP GLYCOSYLATION.
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=23180549; DOI=10.1007/s11274-012-1215-y;
RA Juturu V., Aust C., Wu J.C.;
RT "Heterologous expression and biochemical characterization of acetyl xylan
RT esterase from Coprinopsis cinerea.";
RL World J. Microbiol. Biotechnol. 29:597-605(2013).
CC -!- FUNCTION: Acetylxylan esterase involved in the hydrolysis of xylan, a
CC major structural heterogeneous polysaccharide found in plant biomass
CC representing the second most abundant polysaccharide in the biosphere,
CC after cellulose. Degrades acetylated xylans by cleaving acetyl side
CC groups from the hetero-xylan backbone. {ECO:0000269|PubMed:23180549}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC EC=3.1.1.72; Evidence={ECO:0000269|PubMed:23180549};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.3 mM for 4-nitrophanyl acetate {ECO:0000269|PubMed:23180549};
CC KM=0.11 mM for 4-nitrophanyl butyrate {ECO:0000269|PubMed:23180549};
CC Vmax=2.15 umol/min/mg enzyme 4-nitrophanyl acetate
CC {ECO:0000269|PubMed:23180549};
CC Vmax=0.78 umol/min/mg enzyme 4-nitrophanyl butyrate
CC {ECO:0000269|PubMed:23180549};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:23180549};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:23180549};
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000305|PubMed:23180549}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23180549}.
CC -!- DOMAIN: Has a modular structure: a carbohydrate-binding module (CBM) at
CC the N-terminus, a linker rich in serines, threonines, and prolines, and
CC a C-terminal carbohydrate esterase catalytic module. The genes for
CC catalytic modules and CBMs seem to have evolved separately and have
CC been linked by gene fusion. {ECO:0000305}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:23180549}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family. AxeA
CC subfamily. {ECO:0000305}.
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DR EMBL; AACS02000004; EAU81722.1; -; Genomic_DNA.
DR RefSeq; XP_001840093.1; XM_001840041.1.
DR AlphaFoldDB; A8PB24; -.
DR SMR; A8PB24; -.
DR EnsemblFungi; EAU81722; EAU81722; CC1G_12850.
DR GeneID; 6016718; -.
DR KEGG; cci:CC1G_12850; -.
DR VEuPathDB; FungiDB:CC1G_12850; -.
DR eggNOG; ENOG502QTDU; Eukaryota.
DR InParanoid; A8PB24; -.
DR OMA; PRCAMEA; -.
DR OrthoDB; 1351358at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046555; F:acetylxylan esterase 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 GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR010126; Esterase_phb.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF10503; Esterase_PHB; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF53474; SSF53474; 2.
DR SUPFAM; SSF57180; SSF57180; 1.
DR TIGRFAMs; TIGR01840; esterase_phb; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Serine esterase;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..374
FT /note="Acetylxylan esterase"
FT /id="PRO_0000433970"
FT DOMAIN 23..57
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 58..99
FT /note="Ser/Thr/Pro-rich linker"
FT /evidence="ECO:0000305"
FT REGION 60..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..374
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q4WBW4"
FT COMPBIAS 70..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 374 AA; 39665 MW; 55EDEDC4FC27B7BF CRC64;
MVFSPRLSAF VALVALTNAA TAVPMYGQCG GSGYTGPTQC DPGLVCVKLN DWYSQCQSGG
AQPPVTTTSS PPVTVSPPPS TTTVAPPVAT GPPAPEIPAG QLTQLRSFGN NPSNISMFVY
KPQNVKNRPG LLVALHPCGG TAQQYFSGFP GFRQHADQRG FIVLYGQSPP GSSNCWDIIS
TASLTREGGD DSTGIASAVK YALQNWNVDP EKVFVTGTSS GAMMTNIMAA TYPDLFKAGA
VWAGTAVGCL SANTPQFPPD PCQSGTVIRT PQEWGDRVRR AYPGYNGPWP RMQIWHGTND
FALDHKNLAE QMKQWTNVHN ISQTPTSTSP STPRQGWTKQ VYGNGLVETF SGQGAGHGLP
ESGTEVVAMD FFGL
