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Database: UniProt
Entry: A0A1E3LAN7_9BACL
LinkDB: A0A1E3LAN7_9BACL
Original site: A0A1E3LAN7_9BACL 
ID   A0A1E3LAN7_9BACL        Unreviewed;       843 AA.
AC   A0A1E3LAN7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Arabinan endo-1,5-alpha-L-arabinosidase {ECO:0000313|EMBL:ODP30235.1};
DE            EC=3.2.1.99 {ECO:0000313|EMBL:ODP30235.1};
GN   ORFNames=PTI45_00305 {ECO:0000313|EMBL:ODP30235.1};
OS   Paenibacillus nuruki.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1886670 {ECO:0000313|EMBL:ODP30235.1, ECO:0000313|Proteomes:UP000094578};
RN   [1] {ECO:0000313|EMBL:ODP30235.1, ECO:0000313|Proteomes:UP000094578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TI45-13ar {ECO:0000313|EMBL:ODP30235.1,
RC   ECO:0000313|Proteomes:UP000094578};
RA   Kim S.-J.;
RT   "Genome sequencing of Paenibacillus sp. TI45-13ar, isolated from Korean
RT   traditional nuruk.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODP30235.1}.
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DR   EMBL; MDER01000022; ODP30235.1; -; Genomic_DNA.
DR   RefSeq; WP_069325799.1; NZ_MDER01000022.1.
DR   AlphaFoldDB; A0A1E3LAN7; -.
DR   STRING; 1886670.PTI45_00305; -.
DR   PATRIC; fig|1886670.3.peg.328; -.
DR   Proteomes; UP000094578; Unassembled WGS sequence.
DR   GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd18832; GH43_GsAbnA-like; 1.
DR   Gene3D; 2.40.128.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR046780; aBig_2.
DR   InterPro; IPR032291; Abn2_C.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR006558; LamG-like.
DR   PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR   PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR   Pfam; PF20578; aBig_2; 1.
DR   Pfam; PF16369; GH43_C; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   SMART; SM00560; LamGL; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ODP30235.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ODP30235.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094578};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..843
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038551610"
FT   DOMAIN          705..835
FT                   /note="LamG-like jellyroll fold"
FT                   /evidence="ECO:0000259|SMART:SM00560"
FT   ACT_SITE        53
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        302
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            236
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   843 AA;  91756 MW;  BED6B873ACBE4CB3 CRC64;
     MNKSWIQKAT ALTLMISLTI PAIGFGGATS HAEEYELKQA VTSPTFSNVS VHDPSIIKAG
     GTFYVFGSHI SAAKSQDLMN WTSFANGYTT PGNTIYGDLS KNLAGSFKWA GENDADSKGG
     FSVWAPDVIW NPKYVNADGT KGAYTIYYCT SSTYIRSAIG MAVSQKIEGP YTYVDTMIYS
     GFTKDKAFDN NSTVDKKWTN TNIQTLINQK KLSGESSAWF NADGTYANQN YPNAIDPTIF
     SDTKGKLWMT YGSWSGGIFV LEIDAKTGKP IYPGKDGQTK DGRLIDRYFG TKVAGGYGQS
     GEGPYIQYNK ESGYYYLYMT YGGLAANGGY NMRVFRATKP DGPYQDAKGQ QATWPAQTSN
     VTYGNKLIGN YLWDSKVGDP GYGENFGYVS PGHNSVYTDD KTGQTFLVFH TRFPARGEEH
     ELRIHQMYIN KEGWPVVSPY RYAGETLAKV SEEMVVGDYQ FIDHGNDSSA AIKNTQYIRL
     NKDRTISGEL QGTWQKKGTA DAILTIDGVK YTGVFVKDWN PVTKQYNMTF TALSTNGTMG
     WGSRLVEESD KQVVADVYSD LSLGDVSNVI SNVQLPTVAS RGTSVVWTSS NPAVVSNTGV
     VTRPQAGQAP ANVTLTASIS KGNIKQTKVF QVTVQPFVEA TLTAQYSFEH NLKDTTATFG
     QGTVTGDRLD STVGTITYGT GVSGQSAVFN GTSGIRLPQG LISNNSYSVA VWVKPDQLTT
     YSPAFFGAKD TDHWVSLIPR GATADKAMVW SGTAWYDGVT GVTIPANQWT HLAFSVDEGS
     LTIYVNGVQQ FSGTNFPDIF TGGNASFGLG VNYWDTPFKG QMDELRIYKG SLTPAQLSQL
     AKS
//
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