ID Q1ZSR5_PHOAS Unreviewed; 1066 AA.
AC Q1ZSR5;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Chitodextrinase {ECO:0000313|EMBL:EAS64912.1};
GN ORFNames=VAS14_04313 {ECO:0000313|EMBL:EAS64912.1};
OS Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS CCUG 15956)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS64912.1, ECO:0000313|Proteomes:UP000001603};
RN [1] {ECO:0000313|EMBL:EAS64912.1, ECO:0000313|Proteomes:UP000001603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14 {ECO:0000313|EMBL:EAS64912.1,
RC ECO:0000313|Proteomes:UP000001603};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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:EAS64912.1}.
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DR EMBL; AAOJ01000002; EAS64912.1; -; Genomic_DNA.
DR RefSeq; WP_005368345.1; NZ_CH902600.1.
DR AlphaFoldDB; Q1ZSR5; -.
DR eggNOG; COG3325; Bacteria.
DR eggNOG; COG3693; Bacteria.
DR eggNOG; COG3979; Bacteria.
DR HOGENOM; CLU_002833_13_0_6; -.
DR OrthoDB; 9775889at2; -.
DR Proteomes; UP000001603; 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: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; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1066
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004198718"
FT DOMAIN 329..804
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 988..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 114006 MW; 1394604E558D099B CRC64;
MDNGKHGTMR KGIFTLSTLT MSCLFAFNAQ AAVDCTDLTE WKSDSVYTGG DQVQQAGVAY
KANYWTQNNS PKDNNGPYSQ WVQLDLCSGG EPPIDPPIDP VENAAPTASI TAPTATTAIT
TGETVLIKAN ATDTDGTITK VDFLVDGQVV GSTTTAPYEF SWTATEGVHS LSAMAYDDKN
AASSQASVSV DVAPEGPVNE APTVSVAVSA TSVELGEVVT ITAEAADTDG TVEKVDFYVN
GALVGTAATA PYALEYTTVQ AGNAKIFARA TDDQNKTSDS AVSSVAVNGA VVSNGCRPDG
LYQTEGVNVP YCSIYDEDGR EMMGADHPRR VIGYFTSWRA GDDPQSSYLV NDIPWEQLTH
INYAFVSIGE DGKVNIGDTS DPNNAAVGME WDGVEIDPAL GFKGHFGALA TAKEKHDVKT
LISIGGWAET GGHFGTDGGR AADGGFYTMT TNADGSINHA GIEKFATSAV EMLRKYKFDG
LDIDYEYPTS MAGAGNPYDK EFMEPRRPYL WASYQELMKV LREKLDVASA EDGIHYMLTI
AAPSSGYLLR GMETFDVTKY LDYVNIMSYD LHGAWNDHVG HNAALFDTGK DSELAQWNVY
GTAAYGGIGY LNTDWAYHYF RGSMPAGRIN IGVPYYTRGW QDVKGGDNGL WGRAALPNQS
ECQAGTGEGE KNNCGYGAIG IDNMWHDLDP DGKEMGAGSN PMWHAKNLEQ GIFGSYTAAY
GLDPVNDPQD KLVGSYTRNY DDVAVAPWLW NAEKSVFIST EDKASVSVKA DYVIDKEIGG
IMFWELAGDY NCYLFDANGK RTNTIDATEK ACASGNGEYH MGNAMTKAIY DKFKSATPYG
NTIATGAIPT QAIDIAVNVS GFKVGDQNYP INPTVTFTNN TGTDLPGGTE FQFDIPVSAP
DNAKDQSGGG LKVISSGHTR GDNIGGLDGT MHRVAFTLPK WKTLPAGESY ELDFIYYLPI
SGPANYSVNV DGNEYAFKFE QPSLPIGDLN AGGGNNGGGD SGGNNGSCDS DGLTTYPNWP
QTDWQGTPTH AGSGDEIIHD GAVYKANWWT SSVPGSDGSW TKVCNI
//
