ID C0EDG7_9FIRM Unreviewed; 1679 AA.
AC C0EDG7;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=F5/8 type C domain protein {ECO:0000313|EMBL:EEG30453.1};
GN ORFNames=CLOSTMETH_01894 {ECO:0000313|EMBL:EEG30453.1};
OS [Clostridium] methylpentosum DSM 5476.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=537013 {ECO:0000313|EMBL:EEG30453.1, ECO:0000313|Proteomes:UP000003340};
RN [1] {ECO:0000313|EMBL:EEG30453.1, ECO:0000313|Proteomes:UP000003340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5476 {ECO:0000313|EMBL:EEG30453.1,
RC ECO:0000313|Proteomes:UP000003340};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG30453.1, ECO:0000313|Proteomes:UP000003340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5476 {ECO:0000313|EMBL:EEG30453.1,
RC ECO:0000313|Proteomes:UP000003340};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium methylpentosum (DSM 5476).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-
CC 1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the
CC carbohydrate moieties of glycoproteins.
CC {ECO:0000256|ARBA:ARBA00004071}.
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:EEG30453.1}.
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DR EMBL; ACEC01000062; EEG30453.1; -; Genomic_DNA.
DR STRING; 537013.CLOSTMETH_01894; -.
DR eggNOG; COG1196; Bacteria.
DR eggNOG; COG2273; Bacteria.
DR eggNOG; COG3669; Bacteria.
DR HOGENOM; CLU_240798_0_0_9; -.
DR Proteomes; UP000003340; Unassembled WGS sequence.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:InterPro.
DR GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.2700; -; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 3.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR016286; FUC_metazoa-typ.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR PANTHER; PTHR10030:SF46; ALPHA-L-FUCOSIDASE-RELATED; 1.
DR Pfam; PF01120; Alpha_L_fucos; 1.
DR Pfam; PF13290; CHB_HEX_C_1; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF07554; FIVAR; 4.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS50022; FA58C_3; 2.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000003340};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..41
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 42..1679
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002897817"
FT DOMAIN 949..1044
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1172..1271
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 1679 AA; 185703 MW; 8B40F1F298074F3D CRC64;
MKKEKTMKQK RMNFSRMGKT LVAALLSAAL LLPTVGTAVQ ASDILSSQTE TVQVIRPYIT
GMETVGTELK GMYTYYDVNG RPEAGSSFRW LRCDTKLGVY TEIPGATGSN YTLTPEDAGK
YIRFEVTPRT SDEAGSAQQS WMIGPVLTAE QYERIDNRFD NDNDFMANVN SIQSDIASRL
ANAVYFTVDS EGLHGSEVFY KNNVQGDFDP STKPVVQDGT VYAPAAFFTL LLDAEAPDVE
ATTIDGATYY NLKQAAAVLD KQMWSGDEQQ SEIANFQMEH LGQGLIVLSD TEAIFDPVTD
RDLIDEACNM LYTLRATEEQ MQWFRDAKYG MFLHWDPSSQ IGVEISWDRK AFRPADIGSS
YYNAIDPEYD TLGQTFNPTE YNPDEWMQLA KEAGMKYVVL TTKHHASYSN FFSDYDNHTI
KETPYNQDIV EKYVAAAKKA GLKVGFYYSA RDWYNPNYLT ADHHRYLEYY FGQIQELMTN
YGDIDVMWFD SIGTSSLNQW DPRTLLRRMK QINPDVIVNN RYTAVLAGYD KSPYDVNGDW
YTPEHRLGGF DSSRPWESCM TVTEAPGGGW SYRPNGRVKS VEESVKYLIN NVVNDGNLLY
NIGPMPNGKL NETHADVFRQ VGKWLEPYKE AIYNTRGGPY QNPQWGGSTY RTDENGLETI
YLHVTPLLKG YTPSGNSLQI DAPGNGQTYS SASLVKDGKE VQLTYNEDGI LLTLPEGESW
DAYDTVIRLT PDIAATLASK ISQAQSYADS LTSELLATVR QIVENQVAEA KQVLDSGETS
RYTEQLGLLN NCVQYARSAE ALADAVVSAE QKMESVAVGT NPWECPQYLY DSLQNNISAA
KSLLDAADST AAQFDKSASA LNTAVESLND LMNSLVITFT PDQGRVDNGT TFSMSQSWQE
LNIRYTLDGS EPDVSSAIYQ GEQLTIPAGI MTVKAALFDA NGKKVGATCK HTYLNTENVQ
NLSPLASSVQ ASSIYSESYT GAKACDGNMN TRWATPDGTI TATLELQFDS PQTVNTAQIQ
EYLDSGETTR ISKFAIEYWQ DGGWKQAYTG DKVGANKVFS FAEFTSDRVR LNIESCMNVT
IWEFSLFQLE DSVGVTADKT NLRPNETAQL AVSGQLADGK PITPEMIEDV TYHTDRDDLV
SIDETGKLRI KEFSDEISFA VWADVTFNGK TVTTEKLSFK ASVLGENLAL GKTASASSVY
GGGFEAPKAV DGNDRTRWAS KVSSSYWFEV DFGKEEQVNN IAFQVYSDRS DPVNYEVYTD
FKIQYLKDGT WMDAYDSSSM THQITYPVYN GTESYNNVWI DSSGTVKSTD YLVSFDTVTA
SKIRLFSDNT KKDPSIIEFG AYYVPEQAIV DKSGLDAAIQ QAAEYEGKES EYTADSWAAL
CTALETANTV FDDPDADQET VDAAATALQE AIDGLVKREP VETNKTILKK VLDYAVQAKA
GEEYANVIAS VKASFDAALL AADRVYQDAA ASQAEVDRAW MDLLSEIHKL GFQAGDKTQL
ELLLSYAKTI DLTNYVQQGQ AEYTAALAAA QVCFEDGDAL TNEVNLAAQQ LLDAMMNLRL
KADKSILEEL LVRSGRIDTT LYSAETIDSF LQAKKEAERV FADSESTQQA VDSAADNLER
ALERLLPLEA PAIQGHQGNS TSANGSPKTG DPFSVACILL LAASGSVLLK KKQRPDSNK
//
