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IABF_STRAW
ID   IABF_STRAW              Reviewed;         481 AA.
AC   Q82P90;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Extracellular exo-alpha-(1->5)-L-arabinofuranosidase {ECO:0000305|PubMed:18665359};
DE            EC=3.2.1.55 {ECO:0000269|PubMed:18665359};
DE   Flags: Precursor;
GN   Name=Araf43A {ECO:0000303|PubMed:18665359}; Synonyms=abfA;
GN   ORFNames=SAVERM_1043;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP   SPECIFICITY.
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=18665359; DOI=10.1007/s00253-008-1551-x;
RA   Ichinose H., Yoshida M., Fujimoto Z., Kaneko S.;
RT   "Characterization of a modular enzyme of exo-1,5-alpha-L-
RT   arabinofuranosidase and arabinan binding module from Streptomyces
RT   avermitilis NBRC14893.";
RL   Appl. Microbiol. Biotechnol. 80:399-408(2008).
RN   [4] {ECO:0007744|PDB:3AKF, ECO:0007744|PDB:3AKG, ECO:0007744|PDB:3AKH}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 28-481 IN COMPLEX WITH SUBSTRATE,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-47; ASP-162; ASN-186;
RP   TYR-219; GLU-223 AND LEU-316.
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC   8165 / MA-4680;
RX   PubMed=20739278; DOI=10.1074/jbc.m110.164251;
RA   Fujimoto Z., Ichinose H., Maehara T., Honda M., Kitaoka M., Kaneko S.;
RT   "Crystal structure of an Exo-1,5-{alpha}-L-arabinofuranosidase from
RT   Streptomyces avermitilis provides insights into the mechanism of substrate
RT   discrimination between exo- and endo-type enzymes in glycoside hydrolase
RT   family 43.";
RL   J. Biol. Chem. 285:34134-34143(2010).
CC   -!- FUNCTION: Involved in the degradation of arabinan and is a key enzyme
CC       in the complete degradation of the plant cell wall. Catalyzes only the
CC       cleavage of terminal alpha-(1->5) arabinofuranosyl bonds of arabinan
CC       present in the arabinofuranosyl polysaccharides or oligosaccharides. It
CC       cannot act on other arabinose-containing polysaccharides and
CC       arabinoxylo-oligosaccharides. {ECO:0000269|PubMed:18665359}.
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:0000269|PubMed:18665359};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.5 mM for p-nitrophenyl-alpha-L-arabinofuranoside
CC         {ECO:0000269|PubMed:20739278};
CC         Note=kcat is 6.5 min(-1) with p-nitrophenyl-alpha-L-arabinofuranoside
CC         as substrate. {ECO:0000269|PubMed:20739278};
CC       pH dependence:
CC         Optimum pH is 6.0. Stable from pH 5.0 to pH 6.5.
CC         {ECO:0000269|PubMed:18665359};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:18665359};
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000305|PubMed:18665359}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DOMAIN: Organized into two domains: an N-terminal catalytic domain and
CC       a C-terminal arabinose-binding domain (ABD). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR   EMBL; BA000030; BAC68753.1; -; Genomic_DNA.
DR   PDB; 3AKF; X-ray; 2.20 A; A=28-481.
DR   PDB; 3AKG; X-ray; 1.80 A; A=28-481.
DR   PDB; 3AKH; X-ray; 1.70 A; A=28-481.
DR   PDB; 3AKI; X-ray; 2.00 A; A=28-481.
DR   PDBsum; 3AKF; -.
DR   PDBsum; 3AKG; -.
DR   PDBsum; 3AKH; -.
DR   PDBsum; 3AKI; -.
DR   AlphaFoldDB; Q82P90; -.
DR   SMR; Q82P90; -.
DR   STRING; 227882.SAV_1043; -.
DR   EnsemblBacteria; BAC68753; BAC68753; SAVERM_1043.
DR   KEGG; sma:SAVERM_1043; -.
DR   eggNOG; COG3940; Bacteria.
DR   HOGENOM; CLU_009397_2_1_11; -.
DR   OMA; LFQHRMY; -.
DR   UniPathway; UPA00667; -.
DR   EvolutionaryTrace; Q82P90; -.
DR   Proteomes; UP000000428; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   Gene3D; 2.115.10.20; -; 1.
DR   InterPro; IPR007934; AbfB_ABD.
DR   InterPro; IPR036195; AbfB_ABD_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   Pfam; PF05270; AbfB; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF110221; SSF110221; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..481
FT                   /note="Extracellular exo-alpha-(1->5)-L-
FT                   arabinofuranosidase"
FT                   /id="PRO_5004300134"
FT   REGION          37..336
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255"
FT   REGION          349..479
FT                   /note="ABD"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        47
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305|PubMed:20739278"
FT   ACT_SITE        223
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:20739278"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   BINDING         363..366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   BINDING         457..460
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   BINDING         475
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   SITE            162
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000305|PubMed:20739278"
FT   MUTAGEN         47
FT                   /note="D->A: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   MUTAGEN         47
FT                   /note="D->N: Maintains an extremely weak catalytic
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   MUTAGEN         162
FT                   /note="D->A,N: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   MUTAGEN         186
FT                   /note="N->A,L: Reduces substrate specificity."
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   MUTAGEN         219
FT                   /note="Y->A: Reduces substrate specificity and allows
FT                   hydrolysis of alpha-1,5-linked arabinofuranosyl bonds."
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   MUTAGEN         223
FT                   /note="E->A: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   MUTAGEN         316
FT                   /note="L->A: Reduces substrate specificity and allows
FT                   hydrolysis of alpha-1,5-linked arabinofuranosyl bonds."
FT                   /evidence="ECO:0000269|PubMed:20739278"
FT   STRAND          46..52
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          58..63
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          69..77
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   HELIX           79..83
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          87..91
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          100..110
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          113..121
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          130..136
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   TURN            141..143
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          147..151
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          160..168
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          171..178
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          183..196
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          199..208
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   HELIX           213..215
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          217..219
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          221..230
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          233..241
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          248..255
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   HELIX           263..265
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   TURN            278..281
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          282..292
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          298..310
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   HELIX           315..317
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          322..327
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          344..346
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          351..356
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          360..364
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          367..373
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   HELIX           377..380
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          382..386
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          394..401
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          404..409
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          412..417
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   HELIX           422..427
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          430..434
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   TURN            439..441
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          443..450
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          453..458
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          461..466
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   HELIX           470..475
FT                   /evidence="ECO:0007829|PDB:3AKH"
FT   STRAND          478..480
FT                   /evidence="ECO:0007829|PDB:3AKH"
SQ   SEQUENCE   481 AA;  53105 MW;  61AF442D20B07738 CRC64;
     MRRLTVRLFT AVLAALALLT MGTPAHATAP ASPSVTFTNP LAEKRADPHI FKHTDGYYYF
     TATVPEYDRI VLRRATTLQG LATAPETTIW TKHASGVMGA HIWAPEIHFI DGKWYVYFAA
     GSTSDVWAIR MYVLESGAAN PLTGSWTEKG QIATPVSSFS LDATTFVVNG VRHLAWAQRN
     PAEDNNTSLF IAKMANPWTI SGTPTEISQP TLSWETVGYK VNEGPAVIQH GGKVFLTYSA
     SATDANYCLG MLSASASADL LNAASWTKSS QPVFKTSEAT GQYGPGHNSF TVSEDGKSDI
     LVYHDRNYKD ISGDPLNDPN RRTRLQKVYW NADGTPNFGI PVADGVTPVR FSSYNYPDRY
     IRHWDFRARI EANVTNLADS QFRVVTGLAG SGTISLESAN YPGYYLRHKN YEVWVEKNDG
     SSAFKNDASF SRRAGLADSA DGIAFESYNY PGRYLRHYEN LLRIQPVSTA LDRQDATFYA
     E
 
 
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