ID   AXE7A_PRER2             Reviewed;         439 AA.
AC   D5EXI2;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Acetyl esterase Axe7A;
DE            EC=3.1.1.- {ECO:0000269|PubMed:21742923};
DE   Flags: Precursor;
GN   Name=axe7A {ECO:0000303|PubMed:21742923}; OrderedLocusNames=PRU_2678;
OS   Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=264731;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ADE82554.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000269|PubMed:20585943};
RX   PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RA   Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA   Coutinho P.M., Henrissat B., Nelson K.E.;
RT   "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT   bryantii: insights into their environmental niche.";
RL   Microb. Ecol. 60:721-729(2010).
RN   [2] {ECO:0000305}
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000269|PubMed:21742923};
RX   PubMed=21742923; DOI=10.1128/aem.05321-11;
RA   Kabel M.A., Yeoman C.J., Han Y., Dodd D., Abbas C.A., de Bont J.A.,
RA   Morrison M., Cann I.K., Mackie R.I.;
RT   "Biochemical characterization and relative expression levels of multiple
RT   carbohydrate esterases of the xylanolytic rumen bacterium Prevotella
RT   ruminicola 23 grown on an ester-enriched substrate.";
RL   Appl. Environ. Microbiol. 77:5671-5681(2011).
CC   -!- FUNCTION: Involved in degradation of plant cell wall polysaccharides.
CC       Has acetyl esterase activity towards a broad range of substrates
CC       including xylose-tetraacetate, 4-O-methylumbelliferyl acetate, glucose-
CC       pentaacetate, cephalosporin C, and acetylated xylo-oligosaccharides
CC       smaller than xylo-heptaose. Displays no detectable activity on
CC       polymeric acetylated xylan. {ECO:0000269|PubMed:21742923}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0 with glucose-pentaacetate as substrate. Active from
CC         pH 5.0 to 8.0. {ECO:0000269|PubMed:21742923};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius with glucose-pentaacetate
CC         as substrate. Active from 30 to 50 degrees Celsius. At temperatures
CC         of 30 degrees Celsius and lower, less than 10% of the maximum
CC         activity is left. At 50 degrees Celsius, retains 60% of its maximum
CC         activity. {ECO:0000269|PubMed:21742923};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000269|PubMed:21742923}.
CC   -!- SIMILARITY: Belongs to the carbohydrate esterase 7 family.
CC       {ECO:0000305}.
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DR   EMBL; CP002006; ADE82554.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5EXI2; -.
DR   SMR; D5EXI2; -.
DR   STRING; 264731.PRU_2678; -.
DR   ESTHER; prer2-d5exi2; Acetyl-esterase_deacetylase.
DR   EnsemblBacteria; ADE82554; ADE82554; PRU_2678.
DR   KEGG; pru:PRU_2678; -.
DR   eggNOG; COG3458; Bacteria.
DR   HOGENOM; CLU_050843_0_0_10; -.
DR   OMA; VHFAARG; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000000927; Chromosome.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; 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; IPR008391; AXE1_dom.
DR   InterPro; IPR039069; CE7.
DR   PANTHER; PTHR40111; PTHR40111; 1.
DR   Pfam; PF05448; AXE1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Serine esterase; Signal; Xylan degradation.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..439
FT                   /note="Acetyl esterase Axe7A"
FT                   /id="PRO_0000422403"
FT   ACT_SITE        309
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        391
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        420
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   439 AA;  49867 MW;  4DE64460501A25A5 CRC64;
     MFNFAPKQTT EMKKLLFTLV FVLGSMATAL AENYPYRADY LWLTVPNHAD WLYKTGERAK
     VEVSFCLYGM PQNVEVAYEI GPDMMPATSS GKVTLKNGRA VIDMGTMKKP GFLDMRLSVD
     GKYQHHVKVG FSPELLKPYT KNPQDFDAFW KANLDEARKT PVSVSCNKVD KYTTDAFDCY
     LLKIKTDRRH SIYGYLTKPK KAGKYPVVLC PPGAGIKTIK EPMRSTFYAK NGFIRLEMEI
     HGLNPEMTDE QFKEITTAFD YENGYLTNGL DDRDNYYMKH VYVACVRAID YLTSLPDWDG
     KNVFVQGGSQ GGALSLVTAG LDPRVTACVA NHPALSDMAG YLDNRAGGYP HFNRLKNMFT
     PEKVNTMAYY DVVNFARRIT CPVYITWGYN DNVCPPTTSY IVWNLITAPK ESLITPINEH
     WTTSETNYTQ MLWLKKQVK