ID Q8G7R4_BIFLO Unreviewed; 531 AA.
AC Q8G7R4;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Possible endo-1,5-alpha-L-arabinosidase {ECO:0000313|EMBL:AAN24037.1};
GN OrderedLocusNames=BL0183 {ECO:0000313|EMBL:AAN24037.1};
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN24037.1, ECO:0000313|Proteomes:UP000000439};
RN [1] {ECO:0000313|EMBL:AAN24037.1, ECO:0000313|Proteomes:UP000000439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; AE014295; AAN24037.1; -; Genomic_DNA.
DR RefSeq; NP_695401.1; NC_004307.2.
DR RefSeq; WP_007054128.1; NC_004307.2.
DR AlphaFoldDB; Q8G7R4; -.
DR SMR; Q8G7R4; -.
DR STRING; 206672.BL0183; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR EnsemblBacteria; AAN24037; AAN24037; BL0183.
DR KEGG; blo:BL0183; -.
DR PATRIC; fig|206672.9.peg.1482; -.
DR HOGENOM; CLU_009397_1_2_11; -.
DR OrthoDB; 9801455at2; -.
DR PhylomeDB; Q8G7R4; -.
DR Proteomes; UP000000439; 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 Gene3D; 2.40.128.10; -; 1.
DR InterPro; IPR032291; Abn2_C.
DR InterPro; IPR006710; Glyco_hydro_43.
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; PF16369; GH43_C; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000000439};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..531
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038367062"
FT DOMAIN 405..528
FT /note="Extracellular endo-alpha-(1->5)-L-arabinanase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16369"
FT REGION 32..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 274
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 210
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 531 AA; 58785 MW; F3BFB2EA133A7234 CRC64;
MTLTGTLRKA FATTLAAAML IGTLAGCSSN ANSNASSNAK NSSDSSQTST TEIKRGESHD
PSIVKANGKY YIFGSHLAWL KSDDLVNWTS FKNNLSTDYE KIFADIWTNW SKQSANPDVK
GNMWAPDVIW NATMKKWCMY MSINGANYRS AIVLLTADDI EGDWTYVGPV TYSGFEKVNA
SKTDVWKVLG EGADLTRYTS QTDTGINAID PCVKQGDNGD LWMTFGSWFG GMWMFKLDPK
TGLRDYSTTY QTVKNQSDAY YGIKLGGGFG NSGEGSYLLH TNGHWYLFAS YGNLQQTGGY
QVRMFRADKI TGPYIDENGN AAVSERAIGN NWQSEVGVRL MSSIQWSGND NSHIEVAQGH
NSAFVDDDGT TYIVYHSRFS DTGEMHQVRV RELLPTDDGW LVAAPYEYTG TKAADTKYDA
KNVAGDYEFV IHDQRTSFKG PKKVTDKHST DYRGVNKPVN ITLTEDGKVT GDKTGTWKLD
KSDGTGDMTI TLDGVEYHGA FDRLPRDKDD RKVEMTFSVI GDNLCAWASQ K
//
