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Database: UniProt
Entry: Q87HX4_VIBPA
LinkDB: Q87HX4_VIBPA
Original site: Q87HX4_VIBPA 
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
//
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