ID F4C2R5_SPHS2 Unreviewed; 377 AA.
AC F4C2R5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Glycoside hydrolase family 43 {ECO:0000313|EMBL:ADZ80977.1};
GN OrderedLocusNames=Sph21_4460 {ECO:0000313|EMBL:ADZ80977.1};
OS Sphingobacterium sp. (strain 21).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ80977.1};
RN [1] {ECO:0000313|EMBL:ADZ80977.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=21 {ECO:0000313|EMBL:ADZ80977.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT "Complete sequence of Sphingobacterium sp. 21.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP002584; ADZ80977.1; -; Genomic_DNA.
DR AlphaFoldDB; F4C2R5; -.
DR STRING; 743722.Sph21_4460; -.
DR KEGG; shg:Sph21_4460; -.
DR PATRIC; fig|743722.3.peg.4748; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_4_0_10; -.
DR OrthoDB; 3308423at2; -.
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; cd08991; GH43_HoAraf43-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 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:ARBA00023277};
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 Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..377
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003306176"
FT ACT_SITE 39
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 257
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 162
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 377 AA; 42165 MW; 768167FE9C3707C8 CRC64;
MKRIISIFTF FSLTLSFNNQ LFAQSQNTYQ NPLPVAFGDP YVLHVAGDKY YMYGTGGVAK
NGFAAYSSTD LVNWKDEGQV FYAGNPNGWS DSTAAWNGAY WAPEVYAHNG KFYLFYSAQW
SDNPGKEVEN FRIGVAVADK PTGPFVDLTD KPIFDPGYPI IDANVLFDDS GKIYLYYSRC
CYKHPVESEV ATWAKKKGWF DTIEESWVYG VELKPDFSGV IGEPVLLLRP PVEMSDKQAE
WESRSVTSKE VNRRWTEGSA IFKKGDTYYM MYSANYFGGK NYAVGYATSK SPLGPFTKAA
NNPVLQKNSE HGGVVTGTGH NSVTYSPDGK EMFCVYHART LSTGEERVVF IDRMKITEDG
KLIVEGPTTT PQLVPSR
//
