ID K4KPQ8_SIMAS Unreviewed; 1028 AA.
AC K4KPQ8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN OrderedLocusNames=M5M_14920 {ECO:0000313|EMBL:AFV00119.1};
OS Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Simiduia.
OX NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFV00119.1, ECO:0000313|Proteomes:UP000000466};
RN [1] {ECO:0000313|EMBL:AFV00119.1, ECO:0000313|Proteomes:UP000000466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC {ECO:0000313|Proteomes:UP000000466};
RX PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT bacterium able to degrade a variety of polysaccharides.";
RL Genome Announc. 1:E00039-E00039(2013).
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}.
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DR EMBL; CP003746; AFV00119.1; -; Genomic_DNA.
DR RefSeq; WP_015048271.1; NZ_ATUQ01000010.1.
DR AlphaFoldDB; K4KPQ8; -.
DR STRING; 1117647.M5M_14920; -.
DR KEGG; saga:M5M_14920; -.
DR eggNOG; COG3291; Bacteria.
DR HOGENOM; CLU_008926_0_1_6; -.
DR OrthoDB; 9808897at2; -.
DR Proteomes; UP000000466; Chromosome.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.2810; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF17963; Big_9; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00942; CBM_3; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR Pfam; PF18911; PKD_4; 1.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM01067; CBM_3; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 2.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS51172; CBM3; 1.
DR PROSITE; PS00698; GH9_3; 1.
DR PROSITE; PS50093; PKD; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000000466};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 25..1028
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5005138043"
FT DOMAIN 492..652
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT DOMAIN 847..929
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 922..1028
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT ACT_SITE 448
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 457
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 1028 AA; 108585 MW; AF18FE23AF054382 CRC64;
MKKQYLKKAL FSAVAFAASA GVQAATPNYG EALQKSIYFY EAQQAGKLPA WNRNEWRGDS
VLQDGSDVGV DLSGGWFDAG DHVKFGFPMA ASATLLAWGV LEYPEAYTQA GQMVHIKNNL
RFVADYFVSA HTAPNELYGQ VGSGSADHAW WGSPEVIHLT DRAASTRPSY KIDASCPGSD
LAGETAAALA AISMVFKADD PAYAATLLSH ARELYTFAHT YKGKYSDCIT DAKSFYNSWS
GYNDELVWSA IWLHKATGEA GYLNSAKVAY ANLNTEQQST VKSYKWTHAW DDKGYGSYVL
MAKLTGDAQY EADAERWLDY WTTGYNAARV KYTAGGLAQL DTWGATRYAA NTSFIALIYS
DYLKSKNPAN PRVSTYYNFA KGQLEYILGD NPMGIPYQIG MAANGPKNPH HRGAHGTWAD
SLQNPTDSRH LLVGALVGGP GTGDAYVDDR GDYIANEVAT DYNSGFTGAL ARLYLDFGGN
PIAESQFPAK EVRDLEYFVE AKSNATGPRH IEIAAKVYNR SAWPAANGDK LKFRYFVDLS
AEMAKGYTAA DVTVSTAYSQ ATSVSQLKVW GDPSKNIYYT EVDFTGVNIF PGGQSDHKKE
VQFRLSLPTT GNSPDWVNEG DPSWDSYGAA DKKAPKIALY SGNTLIWGAE PTPACGAGTS
INCAPVADNV TVTTAADTPV AVILKGSDSD GTVASYQVAA PAHGVLSGTG ANRTYTPNNG
FFGVDSFTYT VTDNLGAVSA PATVSVSVSE PVVPSVAISS PANGTTVYTS GSFTLHYALA
NAASVRILVN GGQVASGVTG GTAQLVAPAT VGNFLVEVIA QDSAGNDLSA TSSVTLSAVT
PPANTPPVAS FTLTSAGLTA TANASASSDA DGDPLTYSWS FDGVTKTGVN ANHTFATAGT
YSVALTVSDG IDTDTLIQSV TVTPPVAGVQ CDFVVSNEWN TGFVAVIRLT NNGSAAVNGW
NVSWLFPEGV TRTSGWNATV TGNNPYSATG LSWNSVIQPG QTVEFGMQGS KPDGTAAPVP
TVTGDVCI
//
