ID Q87HX4_VIBPA Unreviewed; 1054 AA.
AC Q87HX4;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE SubName: Full=Chitodextrinase {ECO:0000313|EMBL:BAC62175.1};
GN OrderedLocusNames=VPA0832 {ECO:0000313|EMBL:BAC62175.1};
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC62175.1, ECO:0000313|Proteomes:UP000002493};
RN [1] {ECO:0000313|EMBL:BAC62175.1, ECO:0000313|Proteomes:UP000002493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR EMBL; BA000032; BAC62175.1; -; Genomic_DNA.
DR RefSeq; NP_800342.1; NC_004605.1.
DR RefSeq; WP_005479129.1; NC_004605.1.
DR AlphaFoldDB; Q87HX4; -.
DR DNASU; 1191521; -.
DR GeneID; 1191521; -.
DR KEGG; vpa:VPA0832; -.
DR PATRIC; fig|223926.6.peg.3762; -.
DR eggNOG; COG3325; Bacteria.
DR eggNOG; COG3979; Bacteria.
DR HOGENOM; CLU_002833_13_0_6; -.
DR Proteomes; UP000002493; Chromosome 2.
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; cd12204; CBD_like; 1.
DR CDD; cd12215; ChiC_BD; 1.
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; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR032798; CBM_5_12_2.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR009470; Chi_C.
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:SF308; CHITINASE A; 1.
DR Pfam; PF17957; Big_7; 2.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF14600; CBM_5_12_2; 1.
DR Pfam; PF06483; ChiC; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
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:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000002493};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1054
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004300871"
FT DOMAIN 322..807
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 1054 AA; 111857 MW; 92EE689F138EBE7E CRC64;
MHLKNGKAVK SVFTLSTLTA SCLLAFNSYA AVDCAPLEVW DSSKVYNGGD QVQHEGNAYK
ARYWTQNNNP AQAGQWGEWE SLGACDGTGP VDPPQNEIPT VTLTAPSASA SITAGEVVNL
AADAADTDGT ISKVEFFVDG ALVGQSTSAP FIASWTATEG VHEFSTKSYD DAGAVSTASS
VTLTIASVQP GNEAPTVDVA LSATSIELGG TVTLTANAAD ADGSIAKVDF YVAGALAGTA
TAAPYTLDVT PSKAGALAVY AKATDNAGAS TDSAIATLTV NGGAVASNCR PDGLYQTTGV
DVPYCSIYDE EGREKMGADH PRRVIGYFTS WRAGDDPQST YLVKDIPWEQ LTHINYAFVS
IGSDGKVNVG DVNDPNNAAT GKTWPGVEVD PTLGFKGHFG ALATYKQKHD VKTLISIGGW
AETGGHFDAN GDRVADGGFY TMTTNADGSI NHAGIEKFAA SAVEMMRKYK FDGLDIDYEY
PTSMAGAGNP YDKDFMEPRR QYLWASYQEL MKVLREKLDA ASAQDGTHYM LTIAAPSSGY
LLRGMETFDV TKYLDYVNIM SYDLHGAWND HVGHNAALFD TGKDSELAQW NVYGTAAYGG
IGYLNTDWAY HYFRGSMPAG RINIGVPYYT RGWQGVTGGD NGLWGRAALP NQAECQPGTG
EGEKNNCGNG AIGIDNMWHD LDPQGREMGA GSNPMWHAKN LEKGIWGSYA QAYGLDPVND
PSDKLVGTYT RNYDSVAVAP WLWNAEKGVF LSTEDKASIE VKADYVIDKE IGGIMFWELA
GDYNCYVLDA NGNRTAIDAT EQACAAGNGE YHMGNTMTKA IYDKFKSATP YGNKVATGPT
PTEAVDITVS VGGFKVGDQN YPINPKITFT NNTGQAIPGG TEFQFDIPVS APDNAKDQSG
GGLKVIASGH TRANNIGGLD GVMHRVSFSL PAWKDLPAGG TYELDMVYYL PISGPANYSV
ISGGKEFAFK FEQPDLPIGD LNAGTGGGGT TEPGSCDTAG LVTYPNLPQT DWAGNPSHAN
QGDKVIHNGV VYQANWWTAS EPGSDGSWAT VCNI
//