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ABFB_ASPFN
ID   ABFB_ASPFN              Reviewed;         506 AA.
AC   B8N7I7;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Probable alpha-L-arabinofuranosidase B;
DE            Short=ABF B;
DE            Short=Arabinosidase B;
DE            EC=3.2.1.55;
DE   Flags: Precursor;
GN   Name=abfB; ORFNames=AFLA_104300;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Alpha-L-arabinofuranosidase involved in the degradation of
CC       arabinoxylan, a major component of plant hemicellulose. Able to
CC       hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-
CC       arabinofuranosyl oligosaccharides, but also in polysaccharides
CC       containing terminal non-reducing L-arabinofuranoses in side chains,
CC       like L-arabinan, arabinogalactan and arabinoxylan (By similarity).
CC       {ECO:0000250}.
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   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DOMAIN: Organized into two domains: an N-terminal catalytic domain and
CC       a C-terminal arabinose-binding domain (ABD). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 54 family. {ECO:0000305}.
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DR   EMBL; EQ963475; EED53056.1; -; Genomic_DNA.
DR   RefSeq; XP_002376302.1; XM_002376261.1.
DR   AlphaFoldDB; B8N7I7; -.
DR   SMR; B8N7I7; -.
DR   STRING; 5059.CADAFLAP00004167; -.
DR   EnsemblFungi; EED53056; EED53056; AFLA_104300.
DR   VEuPathDB; FungiDB:AFLA_104300; -.
DR   eggNOG; ENOG502QS3Q; Eukaryota.
DR   HOGENOM; CLU_029332_3_0_1; -.
DR   OMA; HYNGACC; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; ISS:UniProtKB.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019566; P:arabinose metabolic process; ISS:UniProtKB.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
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; PTHR39447; 1.
DR   Pfam; PF05270; AbfB; 1.
DR   Pfam; PF09206; ArabFuran-catal; 1.
DR   SUPFAM; SSF110221; SSF110221; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..506
FT                   /note="Probable alpha-L-arabinofuranosidase B"
FT                   /id="PRO_0000394604"
FT   REGION          27..343
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   REGION          344..506
FT                   /note="ABD"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        229
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        305
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         424
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         426
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         427
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         443
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         471
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         473
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         476
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   BINDING         496
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   SITE            184..185
FT                   /note="Cis-peptide bond"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        29..39
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   DISULFID        89..94
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   DISULFID        184..185
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
FT   DISULFID        409..447
FT                   /evidence="ECO:0000250|UniProtKB:Q8NK89"
SQ   SEQUENCE   506 AA;  52217 MW;  C27B7EE289D8A3AF CRC64;
     MSSGLSLERA CAVALGIVAS ASLVAAGPCD IYSSGGTPCV AAHSTTRALY SAYTGALYQV
     KRGSDGSTTD IAPLSAGGVA DAATQDSFCA NTTCLITIIY DQSGRGNHLT QAPPGGFNGP
     ESNGYDNLAS AVGAPVTLNG KKAYGVFMSP GTGYRNNAAS GTATGDEAEG MYAVLDGTHY
     NSACCFDYGN AEVSNTDTGN GHMEAIYYGD NTVWGSGAGS GPWIMADLEN GLFSGLSSKN
     NAGDPSISYR FVTAVVKGEA NQWSIRGANA ASGSLSTYYS GARPSASGYN PMSKEGAIIL
     GIGGDNSNGA QGTFYEGVMT SGYPSDATEN SVQADIVAAK YAIASLTSGP ALTVGSSISL
     QVTTAGYTTR YLAHDGSTVN TQVVSSSSTT ALKQQASWTV RTGLANSACF SFESVDTPGS
     YIRHYNFALL LNANDGTKQF YEDATFCPQA GLNGQGNSIR SWSYPTRYFR HYENVLYVAS
     NGGVQTFDAT TSFNDDVSWV VSTGFA
 
 
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