ID A0A239IKC9_9BACT Unreviewed; 359 AA.
AC A0A239IKC9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Arabinan endo-1,5-alpha-L-arabinosidase {ECO:0000313|EMBL:SNS94025.1};
GN ORFNames=SAMN05421770_103155 {ECO:0000313|EMBL:SNS94025.1};
OS Granulicella rosea.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=474952 {ECO:0000313|EMBL:SNS94025.1, ECO:0000313|Proteomes:UP000198356};
RN [1] {ECO:0000313|EMBL:SNS94025.1, ECO:0000313|Proteomes:UP000198356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18704 {ECO:0000313|EMBL:SNS94025.1,
RC ECO:0000313|Proteomes:UP000198356};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FZOU01000003; SNS94025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239IKC9; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000198356; Unassembled WGS sequence.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:InterPro.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR026534};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR026534};
KW Reference proteome {ECO:0000313|Proteomes:UP000198356}.
FT ACT_SITE 63
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT ACT_SITE 244
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 183..186
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 203..205
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT SITE 186
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 359 AA; 39087 MW; 356B440F0982C968 CRC64;
MRMVGGAGKT QILRLRCASL RLKGPATIRA ISLSILLFTA ITSTFAQSPE AYRLSGDVAG
AHDPSIIRQG DRWYVFTTGK TRDGGLLGIR CSSDAHEWRL CGHVFDTMPA WIAQRSPGTH
DLWAPDITFA NGVYRLYYCY SLFGKNASGI ALATNKTLDP ASPDYRWVDE GLVLQSRAGD
DFNAIDPAWV ADEQGHGWLT FGSFWSGIQL VRLDDATGKL PTPVTGVMVY PLARRSKEDG
HAVEAPSILH HDGWFYLFTS WDACCRGAKS TYRTVVGRSR RIAGPYLDRS GKPLLEGGGT
ELLTGNARWA GPGGETAYAT ATGDLLVFHA YDATTGKPYL QISPIDWVDG WPKVALGAP
//
