ID   A0A172ZC67_9BACL        Unreviewed;       846 AA.
AC   A0A172ZC67;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Arabinanase {ECO:0000313|EMBL:ANF95234.1};
GN   ORFNames=AR543_03790 {ECO:0000313|EMBL:ANF95234.1};
OS   Paenibacillus bovis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF95234.1, ECO:0000313|Proteomes:UP000078148};
RN   [1] {ECO:0000313|Proteomes:UP000078148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD3526 {ECO:0000313|Proteomes:UP000078148};
RA   Wu Z., Gao C., Liu Z., Zheng H.;
RT   "Genome of Paenibacillus bovis sp. nov.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ANF95234.1, ECO:0000313|Proteomes:UP000078148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD3526 {ECO:0000313|EMBL:ANF95234.1,
RC   ECO:0000313|Proteomes:UP000078148};
RX   PubMed=26769366; DOI=10.1099/ijsem.0.000900;
RA   Gao C., Han J., Liu Z., Xu X., Hang F., Wu Z.;
RT   "Paenibacillus bovis sp. nov., isolated from raw yak (Bos grunniens)
RT   milk.";
RL   Int. J. Syst. Evol. Microbiol. 66:1413-1418(2016).
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}.
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DR   EMBL; CP013023; ANF95234.1; -; Genomic_DNA.
DR   RefSeq; WP_060531969.1; NZ_CP013023.1.
DR   AlphaFoldDB; A0A172ZC67; -.
DR   STRING; 1616788.AR543_03790; -.
DR   KEGG; pbv:AR543_03790; -.
DR   OrthoDB; 9801455at2; -.
DR   Proteomes; UP000078148; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078148};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..846
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038793482"
FT   DOMAIN          706..838
FT                   /note="LamG-like jellyroll fold"
FT                   /evidence="ECO:0000259|SMART:SM00560"
FT   ACT_SITE        52
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        301
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            235
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   846 AA;  92283 MW;  9AFEFA04AA490BE9 CRC64;
     MRKNVTKKLA VATLAFSLAV SAAGVTNNEQ ASAAKVDNPP AEPTFSNATV HDPSIIKTGN
     TFYVFGSHIS AAKSPDLLHW SNFANGYTTP GNTLYGDLSK TLAGSFKWAG ENDADSKGGF
     AVWAPDVIWN PKYVNKDGSK GAYTLYYSTS STYIRSAIGM AVSQKIEGPY EYTDTFIYTG
     FTKDKAFDAN SQVDKKWTNT NIQTLIDQKK ISAENPAWFN ENGSYANQQY PNAIDPTIFY
     DAKGKMWMTY GSWSGGIFVL EVDQKTGKPI YPGKDGKTKD GRMIDRYFGT KIAGGYGKSG
     EGPYIQYNKD SGYFYLYMTY GGLAANGGYN MRVFRSKSAD GPYVDARGHQ ATWPANTSND
     EYGNKLIGNF LFDSKVGDPG KEQDYGYVSP GHNSVYTDPK TGQLFLVFHT RFPGRGEEHE
     LRIHQMFINK EGWPVVSPYR YAGEQEAKVS DKMITGDYQF VDHGSDSSPA IKEASAIRLN
     EDHTITGELQ GTWKKKGTNN AELTIGGKNY TGVFVKDWDP MSKQYVMTFT ALSDQATMGW
     GSRLPDASDT QVIEDVYGEL ELSGTSGITA NLELPTIGSR GTTINWTSSN EQIIAANGQV
     TRPESGSSAV PVTLTARITR GSETRTKIFE VTVLPYTNAQ LTAQYSFDQN LNDSTGQHGA
     GELTGDRLDR PATVSTLTYG TGVHGQSAVL DGTTGIRLPN GLIHSNSYSV SMWVKPEQLN
     LYSPAFFGAA DSDHWISLLP RGTAGDNTML WAGSTPWYDA STGMKIPAGE WSHLAFSVDQ
     GNVTVYVNGK ETFTGTGFPD RFSASDNASF GLGVNYWDTP FKGELDELQV FEGSLTPAQL
     AELSSK
//