CGKA_PSEVC
ID CGKA_PSEVC Reviewed; 397 AA.
AC P43478;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Kappa-carrageenase;
DE EC=3.2.1.83;
DE Flags: Precursor;
GN Name=cgkA;
OS Pseudoalteromonas carrageenovora (Alteromonas carrageenovora).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-30 AND 33-37.
RC STRAIN=ATCC 43555 / DSM 6820 / JCM 8851 / IAM 12662 / NBRC 12985 / NCIMB
RC 302;
RX PubMed=8112578; DOI=10.1016/0378-1119(94)90531-2;
RA Barbeyron T., Henrissat B., Kloareg B.;
RT "The gene encoding the kappa-carrageenase of Alteromonas carrageenovora is
RT related to beta-1,3-1,4-glucanases.";
RL Gene 139:105-109(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 27-297.
RX PubMed=11435116; DOI=10.1016/s0969-2126(01)00612-8;
RA Michel G., Chantalat L., Duee E., Barbeyron T., Henrissat B., Kloareg B.,
RA Dideberg O.;
RT "The kappa-carrageenase of P. carrageenovora features a tunnel-shaped
RT active site: a novel insight in the evolution of Clan-B glycoside
RT hydrolases.";
RL Structure 9:513-525(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-linkages between D-galactose
CC 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans.;
CC EC=3.2.1.83;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR EMBL; X71620; CAA50624.1; -; Genomic_DNA.
DR PIR; I39507; I39507.
DR PDB; 1DYP; X-ray; 1.54 A; A=27-297.
DR PDB; 5OCQ; X-ray; 1.70 A; A/B=26-301.
DR PDBsum; 1DYP; -.
DR PDBsum; 5OCQ; -.
DR AlphaFoldDB; P43478; -.
DR SMR; P43478; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR KEGG; ag:CAA50624; -.
DR BioCyc; MetaCyc:MON-16652; -.
DR BRENDA; 3.2.1.83; 273.
DR EvolutionaryTrace; P43478; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0033918; F:kappa-carrageenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR008263; GH16_AS.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF49373; SSF49373; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS01034; GH16_1; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycosidase;
KW Hydrolase; Periplasm; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:8112578"
FT CHAIN 26..397
FT /note="Kappa-carrageenase"
FT /id="PRO_0000011798"
FT DOMAIN 26..299
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT DOMAIN 316..387
FT /note="BIG2"
FT /evidence="ECO:0000255"
FT ACT_SITE 163
FT /note="Nucleophile"
FT ACT_SITE 165
FT ACT_SITE 168
FT /note="Proton donor"
FT SITE 260
FT /note="Important for substrate recognition"
FT DISULFID 98..268
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:1DYP"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1DYP"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1DYP"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 80..96
FT /evidence="ECO:0007829|PDB:1DYP"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 101..112
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:1DYP"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:1DYP"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1DYP"
FT STRAND 283..296
FT /evidence="ECO:0007829|PDB:1DYP"
SQ SEQUENCE 397 AA; 44224 MW; DA6D47C4682B10EF CRC64;
MKPISIVAFP IPAISMLLLS AVSQAASMQP PIAKPGETWI LQAKRSDEFN VKDATKWNFQ
TENYGVWSWK NENATVSNGK LKLTTKRESH QRTFWDGCNQ QQVANYPLYY TSGVAKSRAT
GNYGYYEARI KGASTFPGVS PAFWMYSTID RSLTKEGDVQ YSEIDVVELT QKSAVRESDH
DLHNIVVKNG KPTWMRPGSF PQTNHNGYHL PFDPRNDFHT YGVNVTKDKI TWYVDGEIVG
EKDNLYWHRQ MNLTLSQGLR APHTQWKCNQ FYPSANKSAE GFPTSMEVDY VRTWVKVGNN
NSAPGEGQSC PNTFVAVNSV QLSAAKQTLR KGQSTTLEST VLPNCATNKK VIYSSSNKNV
ATVNSAGVVK AKNKGTATIT VKTKNKGKID KLTIAVN
