EABF_STRCO
ID EABF_STRCO Reviewed; 475 AA.
AC O54161;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Extracellular exo-alpha-L-arabinofuranosidase;
DE Short=ABF;
DE EC=3.2.1.55;
DE AltName: Full=Arabinosidase;
DE AltName: Full=Arabinoxylan arabinofuranohydrolase;
DE Flags: Precursor;
GN Name=abfB; OrderedLocusNames=SCO5932; ORFNames=SC7H1.02;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Involved in the degradation of xylan and is a key enzyme in
CC the complete degradation of the plant cell wall. It has a specific
CC arabinofuranose-debranching activity on xylan from gramineae. Acts
CC synergistically with the xylanases and binds specifically to xylan.
CC From small arabinoxylo-oligosides (ranging from arabinoxylotriose to
CC arabinoxylohexaose), it liberates arabinose and, after prolonged
CC incubation, the purified enzyme exhibits some xylanolytic activity as
CC well (By similarity). {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 degradation; xylan degradation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydr olase 62 family.
CC {ECO:0000305}.
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DR EMBL; AL939125; CAA16189.1; -; Genomic_DNA.
DR PIR; T35697; T35697.
DR RefSeq; NP_630049.1; NC_003888.3.
DR RefSeq; WP_011030541.1; NZ_VNID01000007.1.
DR PDB; 3WMY; X-ray; 1.40 A; A=38-475.
DR PDB; 3WMZ; X-ray; 1.90 A; A=38-475.
DR PDB; 3WN0; X-ray; 1.90 A; A=38-475.
DR PDB; 3WN1; X-ray; 2.00 A; A=38-475.
DR PDB; 3WN2; X-ray; 2.10 A; A=38-475.
DR PDBsum; 3WMY; -.
DR PDBsum; 3WMZ; -.
DR PDBsum; 3WN0; -.
DR PDBsum; 3WN1; -.
DR PDBsum; 3WN2; -.
DR AlphaFoldDB; O54161; -.
DR SMR; O54161; -.
DR STRING; 100226.SCO5932; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GH62; Glycoside Hydrolase Family 62.
DR GeneID; 1101374; -.
DR KEGG; sco:SCO5932; -.
DR PATRIC; fig|100226.15.peg.6029; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_041805_2_0_11; -.
DR InParanoid; O54161; -.
DR OMA; STYRWNS; -.
DR PhylomeDB; O54161; -.
DR BRENDA; 3.2.1.55; 5998.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000001973; 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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd08987; GH62; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR005193; GH62_arabinosidase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR40631; PTHR40631; 1.
DR Pfam; PF03664; Glyco_hydro_62; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase; Lectin;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..475
FT /note="Extracellular exo-alpha-L-arabinofuranosidase"
FT /id="PRO_0000008036"
FT DOMAIN 39..166
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:3WMY"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:3WMY"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 263..281
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 316..324
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 326..336
FT /evidence="ECO:0007829|PDB:3WMY"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:3WMY"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 361..368
FT /evidence="ECO:0007829|PDB:3WMY"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:3WN1"
FT STRAND 374..381
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 383..395
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 401..413
FT /evidence="ECO:0007829|PDB:3WMY"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:3WMY"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:3WMY"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:3WMY"
FT STRAND 467..473
FT /evidence="ECO:0007829|PDB:3WMY"
SQ SEQUENCE 475 AA; 50046 MW; 47E707FE543CA60D CRC64;
MHRGSLSRGH TSAVLAAVVA ALAALAALLV ATTPAQAAGS GALRGAGSNR CLDVLGGSQD
DGALLQLYDC WGGTNQQWTS TDTGRLTVYG DKCLDVPGHA TAPGTRVQIW SCSGGANQQW
RVNSDGTVVG VESGLCLEAA GAGTANGTAV QLWTCNGGGN QKWTGLTGTP PTDGTCALPS
TYRWSSTGVL AQPKSGWVAL KDFTTVTHNG RHLVYGSTSS GSSYGSMVFS PFTNWSDMAS
AGQNAMNQAA VAPTLFYFAP KNIWVLAYQW GSWPFIYRTS SDPTDPNGWS APQPLFTGSI
SGSDTGPIDQ TLIADGQNMY LFFAGDNGKI YRASMPIGNF PGNFGSSYTT IMSDTKANLF
EGVQVYKVQG QNQYLMIVEA MGANGRYFRS FTASSLSGSW TPQAASEGNP FAGKANSGAT
WTNDISHGDL VRDNPDQTMT VDPCNLQFLY QGKSPNAGGD YNSLPWRPGV LTLRR
