XYNC_FIBSS
ID XYNC_FIBSS Reviewed; 608 AA.
AC P35811; C9RKP6; D9S812;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Endo-1,4-beta-xylanase C;
DE Short=Xylanase C;
DE EC=3.2.1.8;
DE AltName: Full=1,4-beta-D-xylan xylanohydrolase C;
DE Flags: Precursor;
GN Name=xynC; OrderedLocusNames=Fisuc_0362, FSU_0777;
OS Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC Bacteria; Fibrobacteres; Fibrobacterales; Fibrobacteraceae; Fibrobacter.
OX NCBI_TaxID=59374;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-41.
RX PubMed=8244936; DOI=10.1128/jb.175.23.7666-7672.1993;
RA Paradis F.W., Zhu H., Krell P.J., Phillips J.P., Forsberg C.W.;
RT "The xynC gene from Fibrobacter succinogenes S85 codes for a xylanase with
RT two similar catalytic domains.";
RL J. Bacteriol. 175:7666-7672(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19169 / S85;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Weimer P.J.,
RA Stevenson D.M., Boyum J., Brumm P.I., Mead D.;
RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19169 / S85;
RA Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B.,
RA Russell J.B., Cann I.K.O., Mackie R.I., White B.A.;
RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cleaves xylans with the production of xylose, xylobiose and
CC xylo-oligosaccharides.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8;
CC -!- PATHWAY: Glycan degradation; xylan degradation.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000305}.
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DR EMBL; U01037; AAA21848.1; -; Genomic_DNA.
DR EMBL; CP001792; ACX73974.1; -; Genomic_DNA.
DR EMBL; CP002158; ADL26842.1; -; Genomic_DNA.
DR PIR; B53295; B53295.
DR RefSeq; WP_012820204.1; NC_017448.1.
DR AlphaFoldDB; P35811; -.
DR SMR; P35811; -.
DR STRING; 59374.Fisuc_0362; -.
DR CAZy; GH11; Glycoside Hydrolase Family 11.
DR CLAE; XYN11C_FIBSU; -.
DR PRIDE; P35811; -.
DR EnsemblBacteria; ADL26842; ADL26842; FSU_0777.
DR KEGG; fsc:FSU_0777; -.
DR KEGG; fsu:Fisuc_0362; -.
DR PATRIC; fig|59374.8.peg.752; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_448881_0_0_0; -.
DR OrthoDB; 1121261at2; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000000517; Chromosome.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.180; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR018208; GH11_AS_1.
DR InterPro; IPR033119; GH11_AS_2.
DR InterPro; IPR033123; GH11_dom.
DR InterPro; IPR001137; Glyco_hydro_11.
DR Pfam; PF00457; Glyco_hydro_11; 2.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS00776; GH11_1; 1.
DR PROSITE; PS00777; GH11_2; 1.
DR PROSITE; PS51761; GH11_3; 2.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Repeat; Signal; Xylan degradation.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:8244936"
FT CHAIN 26..608
FT /note="Endo-1,4-beta-xylanase C"
FT /id="PRO_0000008006"
FT DOMAIN 40..250
FT /note="GH11 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT DOMAIN 316..514
FT /note="GH11 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT REGION 263..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 237
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT ACT_SITE 409
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT ACT_SITE 501
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
FT CONFLICT 175
FT /note="T -> I (in Ref. 1; AAA21848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 66403 MW; BA5653D842798DC4 CRC64;
MKTFSVTKSS VVFAMALGMA STAFAQDFCS NAQHSGQKVT ITSNQTGKIG DIGYELWDEN
GHGGSATFYS DGSMDCNITG AKDYLCRAGL SLGSNKTYKE LGGDMIAEFK LVKSGAQNVG
YSYIGIYGWM EGVSGTPSQL VEYYVIDNTL ANDMPGSWIG NERKGTITVD GGTYTVYRNT
RTGPAIKNSG NVTFYQYFSV RTSPRDCGTI NISEHMRQWE KMGLTMGKLY EAKVLGEAGN
VNGEVRGGHM DFPHAKVYVK NGSDPVSSSS VKSSSSTDAP KSSSSKGNGN VSGKIDACKD
VMGHEGKETR TQGQNNSSVT GNVGSSPYHY EIWYQGGNNS MTFYDNGTYK ASWNGTNDFL
ARVGFKYDEK HTYEELGPID AYYKWSKQGS AGGYNYIGIY GWTVDPLVEY YIVDDWFNKP
GANLLGQRKG EFTVDGDTYE IWQNTRVQQP SIKGTQTFPQ YFSVRKSARS CGHIDITAHM
KKWEELGMKM GKMYEAKVLV EAGGGSGSFD VTYFKMTDKA HPLAQPEPES SSSEAKVESS
SSTVALHAAP KMELKSGNFQ VFDMQGRFLG TVKLDAGASV AQVLKANFKN AGIYMVKQGN
FMQRVAVK
