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Database: UniProt
Entry: D2TMG5_CITRI
LinkDB: D2TMG5_CITRI
Original site: D2TMG5_CITRI 
ID   D2TMG5_CITRI            Unreviewed;       734 AA.
AC   D2TMG5;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Polysaccharide degrading enzyme {ECO:0000313|EMBL:CBG91179.1};
GN   OrderedLocusNames=ROD_44841 {ECO:0000313|EMBL:CBG91179.1};
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG91179.1, ECO:0000313|Proteomes:UP000001889};
RN   [1] {ECO:0000313|EMBL:CBG91179.1, ECO:0000313|Proteomes:UP000001889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168 {ECO:0000313|EMBL:CBG91179.1,
RC   ECO:0000313|Proteomes:UP000001889};
RX   PubMed=19897651; DOI=10.1128/JB.01144-09;
RA   Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA   Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA   Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT   "The Citrobacter rodentium genome sequence reveals convergent evolution
RT   with human pathogenic Escherichia coli.";
RL   J. Bacteriol. 192:525-538(2010).
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DR   EMBL; FN543502; CBG91179.1; -; Genomic_DNA.
DR   RefSeq; WP_012908408.1; NC_013716.1.
DR   AlphaFoldDB; D2TMG5; -.
DR   STRING; 637910.ROD_44841; -.
DR   CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   KEGG; cro:ROD_44841; -.
DR   eggNOG; COG3325; Bacteria.
DR   eggNOG; COG3979; Bacteria.
DR   HOGENOM; CLU_002833_11_1_6; -.
DR   Proteomes; UP000001889; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd06548; GH18_chitinase; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..734
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003037118"
FT   DOMAIN          161..524
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   734 AA;  80732 MW;  88B94235475B876C CRC64;
     MKLNKLTAAM FIAGMSLTFS SFAATLSMND DANTISGLNS SQMLSKNNGN TWEAWTDASE
     NNFPGSVTVI VAQKDNNAIN SVDYDPAATY GTAGTLVRYN GYYWQSQWWA DPGRIPGSDP
     VWLRVGPIQI QNLATFTFTP YSGQKAADLQ KEGKDKVAAQ RKVIGYFPEW GVYEAHNYFT
     PDKINFSQLT HLNYGFAVIK GGEVVIHDTY KGPELLRQLD KLTEQNGVTN MVSVGGWNNS
     EEGVFEEATR TQEGINKLAD SMIAFMQEWG FDGIDIDWEY PDSDAERANF TSLVQTLRSK
     LDALGLQSDK YFQLSAAVTT NHNNIQYINP ETTAPLLDSV NVMAYDIHGA FDSITGHNAP
     LYANSKDADQ KLNVASTLQE YSSTWKVPKN KLMVGIPYYG RGWGNVAPTE IVKGLPGLFA
     SGSATVHGAW DDEGQFTGTN PYYLLKEYAA SADWTRYWDS ESQVPYLYNA KTKEFLTYDD
     AESVQKKVNF INQNGYGGAI IWDLSGDTPE HELGEIVEGV LNPPSDVKDF TMVNGRVYTM
     IEATAQKKSN RYIVKFNGKY LCESYKGDVL YGTKSSSNGI TTMGCSTNFV LGDKLTVSLE
     SGSPGLSINT GGPILGELVV SEEHLPSAST EPVKGFAYNK ANSRLEAKLE ENAQKGENRY
     VVKKDGKNYI CESYKGSVYY SYKSTKNGVV TMSCPIKLEV GSTYSLSAES NMPGYNPNTK
     GPVLSSFVAT ADMK
//
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