ID   CGIA_ZOBGA              Reviewed;         491 AA.
AC   Q9F284; G0KZI8;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Iota-carrageenase;
DE            EC=3.2.1.157;
DE   Flags: Precursor;
GN   Name=cgiA {ECO:0000312|EMBL:CAC07822.1}; OrderedLocusNames=zobellia_4265;
OS   Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS   NCIMB 13871 / Dsij).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Zobellia.
OX   NCBI_TaxID=63186;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAC07822.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-48 AND 395-399,
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC   {ECO:0000312|EMBL:CAC07822.1};
RX   PubMed=10934194; DOI=10.1074/jbc.m003404200;
RA   Barbeyron T., Michel G., Potin P., Henrissat B., Kloareg B.;
RT   "iota-Carrageenases constitute a novel family of glycoside hydrolases,
RT   unrelated to that of kappa-carrageenases.";
RL   J. Biol. Chem. 275:35499-35505(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij;
RG   Genoscope - CEA;
RT   "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes iota-carrageenans, sulfated 1,3-alpha-1,4-beta
CC       galactans from red algal cell walls, with an inversion of anomeric
CC       configuration. Also active against hybrid iota-/nu-carrageenan, not
CC       active against kappa- or lambda-carrageenans.
CC       {ECO:0000250|UniProtKB:Q9F5I8, ECO:0000269|PubMed:10934194}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of 1,4-beta-D-linkages between D-galactose 4-
CC         sulfate and 3,6-anhydro-D-galactose-2-sulfate in iota-carrageenans.;
CC         EC=3.2.1.157; Evidence={ECO:0000269|PubMed:10934194};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10934194}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 82 family. {ECO:0000305}.
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DR   EMBL; AJ272071; CAC07822.1; -; Genomic_DNA.
DR   EMBL; FP476056; CAZ98400.1; -; Genomic_DNA.
DR   RefSeq; WP_013995588.1; NC_015844.1.
DR   AlphaFoldDB; Q9F284; -.
DR   SMR; Q9F284; -.
DR   STRING; 63186.ZOBELLIA_4265; -.
DR   CAZy; GH82; Glycoside Hydrolase Family 82.
DR   EnsemblBacteria; CAZ98400; CAZ98400; ZOBELLIA_4265.
DR   KEGG; zga:ZOBELLIA_4265; -.
DR   PATRIC; fig|63186.3.peg.4175; -.
DR   HOGENOM; CLU_555168_0_0_10; -.
DR   OMA; GCAYAVR; -.
DR   OrthoDB; 301547at2; -.
DR   BioCyc; MetaCyc:MON-16653; -.
DR   BRENDA; 3.2.1.157; 7557.
DR   Proteomes; UP000008898; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0033952; F:iota-carrageenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..491
FT                   /note="Iota-carrageenase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000065975"
FT   DISULFID        422..490
FT                   /evidence="ECO:0000250|UniProtKB:Q9F5I8"
SQ   SEQUENCE   491 AA;  53395 MW;  AE310457609FC77C CRC64;
     MKLQFKPVYL ASIAIMAIGC TKEVTENDTS EISEVPTELR AAASSFYTPP GQNVRANKKN
     LVTDYGVNHN DQNDDSSKLN LAIKDLSDTG GILTLPKGKY YLTKIRMRSN VHLEIEKGTV
     IYPTKGLTPA KNHRIFDFAS KTEEKIENAS IVGKGGKFIV DLRGNSSKNQ IVADVGNVTN
     FKISNFTIKD EKTIFASILV SFTDKAGNAW PHKGIIENID QANAHTGYGL IQAYAADNIL
     FNNLSCTGGV TLRLETDNLA MKTAKKGGVR DIFATKIKNT NGLTPVMFSP HFMENGKVTI
     DDVTAIGCAY AVRVEHGFIE IFDKGNRASA DAFKNYIEGI LGAGSVEVVY KRNNGRTWAA
     RIANDFNEAA YNHSNPAVSG IKPGKFATSK VTNVKATYKG TGAKLKQAFL SYLPCSERSK
     VCRPGPDGFE YNGPSLGVTI DNTKRDNSLG NYNVNVSTSS VQGFPNNYVL NVKYNTPKVC
     NQNLGSITSC N