ID A0A0H3E4T8_BACA1 Unreviewed; 322 AA.
AC A0A0H3E4T8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Endo-alpha-(1->5)-L-arabinanase {ECO:0000256|PIRNR:PIRNR026534};
DE EC=3.2.1.99 {ECO:0000256|PIRNR:PIRNR026534};
GN OrderedLocusNames=BATR1942_12185 {ECO:0000313|EMBL:ADP33368.1};
OS Bacillus atrophaeus (strain 1942).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=720555 {ECO:0000313|EMBL:ADP33368.1, ECO:0000313|Proteomes:UP000006867};
RN [1] {ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|Proteomes:UP000006867};
RA Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., Bruce D.,
RA Karavis M., McGregor P., Hong C., Park K.H., Akmal A., Feldman A.,
RA Lin J.S., Chang W.E., Higgs B.W., Demirev P., Lindquist J., Liem A.,
RA Fochler E., Tapia R., Bishop-Lilly K., Detter C., Han C., Sozhamannan S.,
RA Rosenzweig C.N., Skowronski E.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADP33368.1, ECO:0000313|Proteomes:UP000006867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1942 {ECO:0000313|EMBL:ADP33368.1,
RC ECO:0000313|Proteomes:UP000006867};
RX PubMed=21464989; DOI=10.1371/journal.pone.0017836;
RA Gibbons H.S., Broomall S.M., McNew L.A., Daligault H., Chapman C.,
RA Bruce D., Karavis M., Krepps M., McGregor P.A., Hong C., Park K.H.,
RA Akmal A., Feldman A., Lin J.S., Chang W.E., Higgs B.W., Demirev P.,
RA Lindquist J., Liem A., Fochler E., Read T.D., Tapia R., Johnson S.,
RA Bishop-Lilly K.A., Detter C., Han C., Sozhamannan S., Rosenzweig C.N.,
RA Skowronski E.W.;
RT "Genomic signatures of strain selection and enhancement in Bacillus
RT atrophaeus var. globigii, a historical biowarfare simulant.";
RL PLoS ONE 6:E17836-E17836(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in
CC (1->5)-arabinans.; EC=3.2.1.99;
CC Evidence={ECO:0000256|PIRNR:PIRNR026534};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834, ECO:0000256|PIRNR:PIRNR026534}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|PIRNR:PIRNR026534}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002207; ADP33368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H3E4T8; -.
DR KEGG; bae:BATR1942_12185; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_5_1_9; -.
DR OrthoDB; 9801455at2; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000006867; Chromosome.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd18829; GH43_BsArb43A-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR026534};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR026534};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..322
FT /note="Endo-alpha-(1->5)-L-arabinanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002607992"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT ACT_SITE 214
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 159..162
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 179..181
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
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:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 322 AA; 35248 MW; 0C25ECDDB2DCDE66 CRC64;
MKKRRFKRLF HFSYAALTAG LLLTSASPAS AAFWGASNEL LHDPTMVKEG SSWYAFGTGL
TEEKGLRVLK SSDGKKWSVQ KSVFSTPLSW WGNYVPNYEK NQWAPDIQYY NGKYWLYYSV
STFGSNTSAI GLASATSVSS GSWKDEGLVI RSTSANNYNA IDPELTIDKD GNPWLAFGSF
WSGIKLTKLN KDTMKPTGSL YSIAARPNNS GALEAPTITY QNGYYHLMVS FDKCCAGVNS
TYKIAYGRSA NITGPYLDKN GKSMLDGGGT ILDSGNGQWK GPGGQDIVNG NILVRHAYDA
NNSGIPKLLI NDLNWSSGWP SY
//
