ID C3QRP9_9BACE Unreviewed; 633 AA.
AC C3QRP9;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Glycosyl hydrolase, family 43 {ECO:0000313|EMBL:EEO54481.1};
GN ORFNames=BSCG_01406 {ECO:0000313|EMBL:EEO54481.1};
OS Bacteroides sp. 2_2_4.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=469590 {ECO:0000313|EMBL:EEO54481.1};
RN [1] {ECO:0000313|EMBL:EEO54481.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_2_4 {ECO:0000313|EMBL:EEO54481.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., Lander E.,
RA Nusbaum C., Ilzarbe M., Galagan J., Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 2_2_4.";
RL Submitted (DEC-2008) 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}.
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DR EMBL; EQ973357; EEO54481.1; -; Genomic_DNA.
DR RefSeq; WP_004296573.1; NZ_EQ973357.1.
DR AlphaFoldDB; C3QRP9; -.
DR HOGENOM; CLU_445279_0_0_10; -.
DR Proteomes; UP000003969; 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; cd18616; GH43_ABN-like; 1.
DR Gene3D; 2.60.40.1740; hypothetical protein (bacova_03559); 2.
DR InterPro; IPR013728; BT_3987-like_N.
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; PF08522; DUF1735; 2.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EEO54481.1}.
FT DOMAIN 61..164
FT /note="BT-3987-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08522"
FT DOMAIN 206..300
FT /note="BT-3987-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08522"
FT ACT_SITE 330
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 498
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 446
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 633 AA; 70404 MW; F815F1709ED841FF CRC64;
MNYNSIKKNI REIGLMFLSA GLLLFLSCGS DDTKDVSSED GDVNSNQYLQ VQPNGLNVIK
VSSSDVAQVV YPFSVELKGG SASVALTAQL EAWNEKDLEA YNKEEETAYK LLPSSLYSIS
TPQITLEQGI ASKKVEVKFA PDKVFTEFKK NGTEYVIALR LTSSVAKVRK SQSDFLLHIS
FDYPTVSLVM PSQEISVSKM SMPVSVDATF NCRADGEIKT NPWNFTCTLA VPSNAEELVA
KYNEDYKTSY RLLPSANYDL GEGISFKAGE NEATGGITVK REGMEAVKYL LPVQLREASH
ESVALHNEIC YFKIGMTYTN PVITFSSVAD PTVIRTDEGF YLYATQTNSY WIPIYFSKDL
VNWEFKRSAF RKATRPTEDV LPGGGAFWAP EIRYINGKYV LYFSWAKWGD GSISYTAVAT
SDSPVGDFLN AKPLLITDDF GSNCIDQFYY EEDGKKYMFV GSFNGIYVTE LTDDGLSVKR
GADGKPVLKK QVCGRAFEGT NIYKKGKYYY LFASINNCCP NNGMDSKYKV VVGRSENLLG
PYVDRKGKDM LDNSWELVLE GDGETFFGPG HNSIIIPDDA GTDWMIYHSY VKENGTVGGR
LGMLDRIVWS ADGWPTIKKC VPSKGDLLPV FNN
//
