ID   CGLA_PSEVC              Reviewed;         942 AA.
AC   Q0JRK4;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Lambda-carrageenase {ECO:0000312|EMBL:CAL37005.1};
DE            EC=3.2.1.162;
DE   Flags: Precursor;
GN   Name=cglA {ECO:0000312|EMBL:CAL37005.1};
OS   Pseudoalteromonas carrageenovora (Alteromonas carrageenovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=227;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAL37005.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-41; 338-345 AND
RP   487-498, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 43555 / DSM 6820 / JCM 8851 / IAM 12662 / NBRC 12985 / NCIMB
RC   302;
RX   PubMed=17269933; DOI=10.1042/bj20061359;
RA   Guibet M., Colin S., Barbeyron T., Genicot S., Kloareg B., Michel G.,
RA   Helbert W.;
RT   "Degradation of lambda-carrageenan by Pseudoalteromonas carrageenovora
RT   lambda-carrageenase: a new family of glycoside hydrolases unrelated to
RT   kappa- and iota-carrageenases.";
RL   Biochem. J. 404:105-114(2007).
CC   -!- FUNCTION: Hydrolyzes lambda-carrageenan with inversion of anomeric
CC       configuration. Does not hydrolyze iota- and kappa-carrageenans, agarose
CC       or porphyran. {ECO:0000250|UniProtKB:Q05JY7,
CC       ECO:0000269|PubMed:17269933}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-linkages in the backbone of
CC         lambda-carrageenan, resulting in the tetrasaccharide alpha-D-
CC         Galp2,6S2-(1->3)-beta-D-Galp2S-(1->4)-alpha-D-Galp2,6S2-(1->3)-D-
CC         Galp2S.; EC=3.2.1.162; Evidence={ECO:0000269|PubMed:17269933};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q05JY7}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17269933}.
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; AM397269; CAL37005.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0JRK4; -.
DR   SMR; Q0JRK4; -.
DR   BioCyc; MetaCyc:MON-16657; -.
DR   BRENDA; 3.2.1.162; 273.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0033957; F:lambda-carrageenase activity; IDA:UniProtKB.
DR   GO; GO:0102255; F:neo-lambda-carrahexaose hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IDA:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF13360; PQQ_2; 1.
DR   SUPFAM; SSF50998; SSF50998; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:17269933"
FT   CHAIN           26..942
FT                   /note="Lambda-carrageenase"
FT                   /evidence="ECO:0000269|PubMed:17269933"
FT                   /id="PRO_5000080729"
SQ   SEQUENCE   942 AA;  105638 MW;  9741CCC215B0C829 CRC64;
     MKIKILSAMV ASSLLIGCVI PTVKASQSAI KSIETNRTIT KVRTGMLSGG SSIITTSYEG
     TVAAYKFNGE KLWENELSGF MNHDIWVQDI NGDGLVEIFA ANADGNVYCI NSDGSLKWTF
     GLNEVPMNSV TVISDADKKY VVAGGYDKNL YYISTNGELL KTIESGTYSE EGVFGDGVKP
     EARTHTVNFV RPVKSSDGTE KLVVLGTNNS LQSSGRFYIF EPFADLPSEK SRISIKKGIG
     DLRTVDFDND GNDELTLGNS AQIGDAAISV MNLDDLSQKK SQINDIARRI DRFGYRVAQT
     EVVMNEGTPT YLTLFGSRIL LTPESFDVND SEILANKYSY YDMWKDKSSN KLVLASAQSG
     GSQVHIIDTS NPSWKSAYEE LEPQGKLAAI QENTRAIERQ LSNFQKPTRE RAPLPVYFIS
     ESRNEIPTTI ERSEFLYDSP VFLNYSTLPN VENWDRSEVL ADNPKYRDKR DRRKNYTLSS
     EEMFNKLSAG YDNSDGISQW AGHGNDPYMI SLATMKRIIS SGDGKKTVNI YPEIEGHGDA
     FNKVLSDHFY PLAEFSSENN ANLFMRNKHT FWQSTIYAPE WSELRSGRLA DAFVPAMEET
     TDKSMEMSVA GRMGLWAAGS VDNWGERYAR DNPSFDRLRQ HSHQMVPNHA LRQIIYKIAS
     GARYINNFGF NQEYMSLAWE LIGKGALYVP KREELLSLSP VHISMKEPDP IYRETSNNVK
     WTTFYDEEKD SIPYVFSRLN GTWPGAKTLP WDYSNYAADT KERRLDFIPK FPKGLVLITP
     VQQGKFKDEG TVRGTLADNM HPIYKDIMKE YITDGKNYYN PNGEQVMAAD SVRYRQIKNK
     IEEKSNLLPM TVSGEAAWVV AQSAEKHLRL TLVDSGYLNP SNKVAKVKFN SVTPVAIVDV
     LSGETFSPDS NGVVEIPVLA GAFRFIDVKI TEDLRNMQSS TL