CGIA_ALTMA
ID CGIA_ALTMA Reviewed; 491 AA.
AC Q9F5I8;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Iota-carrageenase;
DE EC=3.2.1.157;
DE Flags: Precursor;
GN Name=cgiA {ECO:0000312|EMBL:CAC07801.1};
OS Alteromonas macleodii (Pseudoalteromonas macleodii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=28108;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAC07801.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
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] {ECO:0000305}
RP FUNCTION.
RX PubMed=20227066; DOI=10.1016/j.carres.2010.02.014;
RA Jouanneau D., Boulenguer P., Mazoyer J., Helbert W.;
RT "Enzymatic degradation of hybrid iota-/nu-carrageenan by Alteromonas fortis
RT iota-carrageenase.";
RL Carbohydr. Res. 345:934-940(2010).
RN [3] {ECO:0000305, ECO:0000312|PDB:1H80}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 28-491, AND DISULFIDE BONDS.
RX PubMed=11493601; DOI=10.1074/jbc.m100670200;
RA Michel G., Chantalat L., Fanchon E., Henrissat B., Kloareg B., Dideberg O.;
RT "The iota-carrageenase of Alteromonas fortis. A beta-helix fold-containing
RT enzyme for the degradation of a highly polyanionic polysaccharide.";
RL J. Biol. Chem. 276:40202-40209(2001).
RN [4] {ECO:0000305, ECO:0000312|PDB:1KTW}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-491 IN COMPLEX WITH SUBSTRATE,
RP AND DISULFIDE BONDS.
RX PubMed=14623184; DOI=10.1016/j.jmb.2003.09.056;
RA Michel G., Helbert W., Kahn R., Dideberg O., Kloareg B.;
RT "The structural bases of the processive degradation of iota-carrageenan, a
RT main cell wall polysaccharide of red algae.";
RL J. Mol. Biol. 334:421-433(2003).
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:Q9F284, ECO:0000269|PubMed:10934194,
CC ECO:0000269|PubMed:20227066}.
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:0000250|UniProtKB:Q9F284}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 82 family. {ECO:0000305}.
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DR EMBL; AJ272076; CAC07801.1; -; Genomic_DNA.
DR PDB; 1H80; X-ray; 1.60 A; A/B=28-491.
DR PDB; 1KTW; X-ray; 2.00 A; A/B=28-491.
DR PDB; 3LMW; X-ray; 2.60 A; A/B=27-491.
DR PDBsum; 1H80; -.
DR PDBsum; 1KTW; -.
DR PDBsum; 3LMW; -.
DR AlphaFoldDB; Q9F5I8; -.
DR SMR; Q9F5I8; -.
DR DrugBank; DB01981; 3,6-Anhydro-2-(hydrogen sulfate)-alpha-D-galactopyranose.
DR CAZy; GH82; Glycoside Hydrolase Family 82.
DR KEGG; ag:CAC07801; -.
DR BRENDA; 3.2.1.157; 12273.
DR EvolutionaryTrace; Q9F5I8; -.
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; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..491
FT /note="Iota-carrageenase"
FT /evidence="ECO:0000255"
FT /id="PRO_5000065977"
FT DISULFID 269..298
FT /evidence="ECO:0000269|PubMed:11493601,
FT ECO:0000269|PubMed:14623184"
FT DISULFID 336..360
FT /evidence="ECO:0000269|PubMed:11493601,
FT ECO:0000269|PubMed:14623184"
FT DISULFID 408..476
FT /evidence="ECO:0000269|PubMed:11493601,
FT ECO:0000269|PubMed:14623184"
FT DISULFID 412..484
FT /evidence="ECO:0000269|PubMed:11493601,
FT ECO:0000269|PubMed:14623184"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1H80"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1H80"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 166..178
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 197..213
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 219..245
FT /evidence="ECO:0007829|PDB:1H80"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 258..279
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 288..299
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:1KTW"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:3LMW"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:1KTW"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:3LMW"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:1H80"
FT HELIX 358..367
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 376..386
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:1H80"
FT HELIX 395..402
FT /evidence="ECO:0007829|PDB:1H80"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 448..457
FT /evidence="ECO:0007829|PDB:1H80"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:1H80"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:1H80"
FT HELIX 486..489
FT /evidence="ECO:0007829|PDB:1H80"
SQ SEQUENCE 491 AA; 54795 MW; D5912275F06992CF CRC64;
MRLYFRKLWL TNLFLGGALA SSAAIGAVSP KTYKDADFYV APTQQDVNYD LVDDFGANGN
DTSDDSNALQ RAINAISRKP NGGTLLIPNG TYHFLGIQMK SNVHIRVESD VIIKPTWNGD
GKNHRLFEVG VNNIVRNFSF QGLGNGFLVD FKDSRDKNLA VFKLGDVRNY KISNFTIDDN
KTIFASILVD VTERNGRLHW SRNGIIERIK QNNALFGYGL IQTYGADNIL FRNLHSEGGI
ALRMETDNLL MKNYKQGGIR NIFADNIRCS KGLAAVMFGP HFMKNGDVQV TNVSSVSCGS
AVRSDSGFVE LFSPTDEVHT RQSWKQAVES KLGRGCAQTP YARGNGGTRW AARVTQKDAC
LDKAKLEYGI EPGSFGTVKV FDVTARFGYN ADLKQDQLDY FSTSNPMCKR VCLPTKEQWS
KQGQIYIGPS LAAVIDTTPE TSKYDYDVKT FNVKRINFPV NSHKTIDTNT ESSRVCNYYG
MSECSSSRWE R
