ID A0A2S6IGR1_9ACTN Unreviewed; 789 AA.
AC A0A2S6IGR1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=CLV92_11027 {ECO:0000313|EMBL:PPK93399.1};
OS Kineococcus xinjiangensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Kineococcus.
OX NCBI_TaxID=512762 {ECO:0000313|EMBL:PPK93399.1, ECO:0000313|Proteomes:UP000239485};
RN [1] {ECO:0000313|EMBL:PPK93399.1, ECO:0000313|Proteomes:UP000239485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22857 {ECO:0000313|EMBL:PPK93399.1,
RC ECO:0000313|Proteomes:UP000239485};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|RuleBase:RU361166};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000256|PROSITE-ProRule:PRU10060, ECO:0000256|RuleBase:RU361166}.
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:PPK93399.1}.
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DR EMBL; PTJD01000010; PPK93399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6IGR1; -.
DR OrthoDB; 9808897at2; -.
DR Proteomes; UP000239485; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02850; E_set_Cellulase_N; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR004197; Cellulase_Ig-like.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS00698; GH9_3; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU10060};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU10060};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Reference proteome {ECO:0000313|Proteomes:UP000239485};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 36..789
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5017852797"
FT DOMAIN 37..123
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 184..267
FT /note="Cellulase Ig-like"
FT /evidence="ECO:0000259|Pfam:PF02927"
FT DOMAIN 277..770
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT REGION 702..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 749
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 758
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 789 AA; 84280 MW; 16CF329F669E53FF CRC64;
MPLNHHRKRR AGALTAATAL LVPSALVLAP TPALAADQIT NGDFSDGTAG WTIYPNPSVL
DGAGCNTVPA GSGPYSAAIQ QDVPLVAGEE YRLSFRARST PQIQGPVRVV VQENGGSYEQ
FLPAEKPTFT EAFGEHEFFF TASRSLTAQL AIQQDITNPV AYTICVDDVV LEGGAEAPQY
QPDTGPRVRV NQETYLPQGP KGATLVTDST SALPWQLRDG SGRVVATGTT TPRGVDPTAA
LNVHTIDFGG HRSAGTGFTL TADGETSHPF DIGAAAYERL RDDSKTFFHT NRSGIAISDA
LVPGYGREAG HVGVAPNTGD TAVPCQRLDD DSQELLVGQG DEPWTCDYTS DVTGGWYDAG
DHGKYVVNGG IAVAQLMQEY ERSLTAPTAD RGALGDGTLR IPEAGNGVPD LLDEARWELE
WFLKMQVQPG RPLEGMVFHK VADVDWTGLP LAPADDPQER VLYRPSTAAT LNVAATAAQG
ARLFAPYDEE FSQRLLAAAR TAYAAAQANP ALYAPAPDGA LDPNPGSGPY NDRDVSDEFY
WAAVELYLTT GEPQFRKDVL RSPVHTADVF GPGGFDWGHV APLARMDLAT VPSRLNTAEL
RRARASVLAA ADRYLADQAA QPFGQAYAPG DGNYVWGSNA QVLNNMQVLG TAFDLSGETR
YRDAVVRSMD YLLGRNALNL SYITGYGDVD VRNQHSRMYA NQVDPSLPNP PAGTVSGGPN
STALATGDPI ALKHLQEQCA TAAQLCFIDD IGSWSTNEIT VNWNAPLSWV SSFLADQDNG
DDRGSARKH
//
