ID A0A2M9BRK9_9BACT Unreviewed; 861 AA.
AC A0A2M9BRK9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Chitinase {ECO:0000313|EMBL:PJJ60568.1};
GN ORFNames=CLV45_1997 {ECO:0000313|EMBL:PJJ60568.1};
OS Hymenobacter chitinivorans DSM 11115.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1121954 {ECO:0000313|EMBL:PJJ60568.1, ECO:0000313|Proteomes:UP000228535};
RN [1] {ECO:0000313|EMBL:PJJ60568.1, ECO:0000313|Proteomes:UP000228535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11115 {ECO:0000313|EMBL:PJJ60568.1,
RC ECO:0000313|Proteomes:UP000228535};
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 (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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:PJJ60568.1}.
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DR EMBL; PGFA01000001; PJJ60568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9BRK9; -.
DR OrthoDB; 9775889at2; -.
DR Proteomes; UP000228535; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd12215; ChiC_BD; 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 Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR003610; CBM_fam5/12.
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 InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF17957; Big_7; 2.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 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 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
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:ARBA00023024}.
FT DOMAIN 58..519
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 613..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 91378 MW; FB9EC0C435FDF259 CRC64;
MKTLPLLRLA EARPRLAQKV GPGKRLLGLL ALLLCLLPGL LRAQVSPTVP KKRTDHNKQI
IGYLTQWGPW KDIPGLIPKG SLNQLNVDYS QYTILNFSFF GVAVDGSIHS GDYRNPNIAQ
PGSVQQPAPL VNSDTYSSWD LYLLQGELDL IQYISDGSYA YSLGYRNAAG GWSNVSTGAM
GAFPLALHKQ NGKLGLIDLA HQQGVKVMAS IGGWSMSKHF GDMAADPTKR ARFVSDCQKL
IALGFDGIDL DWEYPGQEGM NFTGQAQDYP NFAVLVEAIR TAVGPNKLIT AAFTAVPSRF
SQFDWVRLNR SMDYFNFMTY DYNGGWSSKA GHNSPLYDYP GAEAANFSLD ATTRGIKAAG
IPLSKVNLGV AFYGRGVVTS GPAALNAPTV KRPETVTPDG QVSTSADFTN WPKDVWDGTP
NYQAILAQTA SWTEYWDDNA KVPYKTNGSY FLSYDNERSV GLKAQYVKDQ QLAGVIVWSA
SGDWLDLAVN TTTYGGKLVS SPNTKAPLVN KLNEVFGAGT VANTPPTVSL TSPASNATFA
APASITITAN AADANGTVSK VEFYQGTTKL GEDLTAPYSF SWSSVAAGTY SLTARATDNA
GAATTSAAVT ITVTGSTTPN TPPTVSLTGP TSGSSYTAPA TINLTANAAD ANGTVSKVEF
YNGATLLGTD TSSPYSFSWS SVAAGTYSLT ARATDNAGAT TTSAAVSVTV TSGSGGCTVA
AWSATAVYTK DMQASRNGNL YVAKWWTQNE DPLTASCQYC PWQLVGPCAS ARTAASASVA
AEALTVFPNP VLTGNKLTLD LGRRYDQVEL ELTGISGGKS YRVAAKNTRT VELTLPALPK
GVVVLQVRAD GQTFTKRLLN Q
//
