ID R5Q0Y5_9BACT Unreviewed; 329 AA.
AC R5Q0Y5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Arabinan endo-1 5-alpha-L-arabinosidase A {ECO:0000313|EMBL:CCZ14802.1};
GN ORFNames=BN679_01670 {ECO:0000313|EMBL:CCZ14802.1};
OS Prevotella sp. CAG:487.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262928 {ECO:0000313|EMBL:CCZ14802.1, ECO:0000313|Proteomes:UP000018275};
RN [1] {ECO:0000313|EMBL:CCZ14802.1, ECO:0000313|Proteomes:UP000018275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:487 {ECO:0000313|Proteomes:UP000018275};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:CCZ14802.1}.
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DR EMBL; CAZM010000234; CCZ14802.1; -; Genomic_DNA.
DR AlphaFoldDB; R5Q0Y5; -.
DR Proteomes; UP000018275; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd18827; GH43_XlnD-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR PANTHER; PTHR43772:SF7; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04480)-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000018275};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..329
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004400736"
FT SITE 157
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 329 AA; 37156 MW; EB7DD0CBC215E69E CRC64;
MRKLLLTSAM ILAVAAGAQA GTKKTKTSGN PIFKGWYADP EGAVLDGAYW IFPTYSAEYD
EQTFMDAFSS KDLVNWTKHP RVLEKKNVSW ARRAMWAPAI IHANDKYYLF FGANDIQNNN
ETGGIGVATA DKPEGPYKDA LGKPLIDKII NGAQPIDQFV FRDDDGEYYM YYGGWGHCNM
VRMSPDLLSI RPFEDGTTYK EVTPENYVEG PFMLKRKGKY YFMWSEGGWG GPDYCVAYAI
ADSPFGPFKR VGKILQQDPE VATGAGHHSV IQVPGKDEWY IVYHRRPLTE KGRDSRVVCI
DRMYFDENGY IKPVKITFEG VKPVKAPKK
//
