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 13-SEP-2023, entry version 116. DE RecName: Full=Kappa-carrageenase; DE EC=3.2.1.83; DE Flags: Precursor; GN Name=cgkA; OS Pseudoalteromonas carrageenovora (Alteromonas carrageenovora). OC Bacteria; Pseudomonadota; 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 / RC NCIMB 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:MONOMER-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 CDD; cd02177; GH16_kappa_carrageenase; 1. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.60.40.1080; -; 1. 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 PANTHER; PTHR10963:SF55; GH16 DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1. DR Pfam; PF02368; Big_2; 1. DR Pfam; PF00722; Glyco_hydro_16; 1. DR SMART; SM00635; BID_2; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 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 //