ID C1DQS5_AZOVD Unreviewed; 417 AA.
AC C1DQS5;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Alginate lyase {ECO:0000313|EMBL:ACO77598.1};
GN Name=alyA3 {ECO:0000313|EMBL:ACO77598.1};
GN OrderedLocusNames=Avin_13810 {ECO:0000313|EMBL:ACO77598.1};
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO77598.1, ECO:0000313|Proteomes:UP000002424};
RN [1] {ECO:0000313|EMBL:ACO77598.1, ECO:0000313|Proteomes:UP000002424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX PubMed=19429624; DOI=10.1128/JB.00504-09;
RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
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DR EMBL; CP001157; ACO77598.1; -; Genomic_DNA.
DR AlphaFoldDB; C1DQS5; -.
DR STRING; 322710.Avin_13810; -.
DR CAZy; PL7; Polysaccharide Lyase Family 7.
DR EnsemblBacteria; ACO77598; ACO77598; Avin_13810.
DR KEGG; avn:Avin_13810; -.
DR eggNOG; COG2931; Bacteria.
DR HOGENOM; CLU_658335_0_0_6; -.
DR OMA; HETNFLY; -.
DR Proteomes; UP000002424; Chromosome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 1.
DR InterPro; IPR014895; Alginate_lyase_2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR InterPro; IPR019960; T1SS_VCA0849.
DR NCBIfam; TIGR03661; T1SS_VCA0849; 1.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF08787; Alginate_lyase2; 1.
DR Pfam; PF00353; HemolysinCabind; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Lyase {ECO:0000313|EMBL:ACO77598.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 1..184
FT /note="Alginate lyase 2"
FT /evidence="ECO:0000259|Pfam:PF08787"
FT REGION 189..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 43670 MW; 53584CBAB115FAC7 CRC64;
MVFSAMVNGA TTSGSKYARS ELREMKGSER AAWKLSEGGT MTATLEVDKV PQKSDGSPGR
VVVGQIHGQD EELVRLYYEN GKVYFVNDRA GSKNTETTFA LKDANGNEPN VSLNEKFSYK
IDAKSDELTV EVYADGNTYT STSKISSVWQ SDKFYFKAGA YLGVNDSSGS GSAQVSFYGL
DFSHTDGGGL AGLQEQTTKS TSTSTSTASS AVTDTESQSS STTGSSSSTS STSSASSTSA
TLKGDDKANS LTGTKENDVI RANGGDDKVY GRDGNDELYG NSGNDKLYGN AGDDKLYGTA
GDDVLQGGPG KDLLEGGSGA DKFVFTSLED AGDTITDFRS GDVIDISSLV EDFSRGGDDM
SLKDLKSNGF INFKETTDNT YEVHVDADGA KGSAADVTLV TVVGVDDSVT DTSALIV
//