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CGLA_PSEAS
ID   CGLA_PSEAS              Reviewed;         942 AA.
AC   Q05JY7;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Lambda-carrageenase {ECO:0000312|EMBL:BAF35571.1};
DE            EC=3.2.1.162;
DE   Flags: Precursor;
GN   Name=cglA {ECO:0000312|EMBL:BAF35571.1};
OS   Pseudoalteromonas sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=53249;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAF35571.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-45; 231-242 AND
RP   604-614, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=CL19 {ECO:0000312|EMBL:BAF35571.1};
RX   PubMed=16926183; DOI=10.1093/jb/mvj180;
RA   Ohta Y., Hatada Y.;
RT   "A novel enzyme, lambda-carrageenase, isolated from a deep-sea bacterium.";
RL   J. Biochem. 140:475-481(2006).
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:Q0JRK4,
CC       ECO:0000269|PubMed:16926183}.
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:16926183};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:16926183};
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius. Retains significant
CC         activity in the low temperature range (less than 10 degrees Celsius).
CC         {ECO:0000269|PubMed:16926183};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16926183}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16926183}.
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DR   EMBL; AB261169; BAF35571.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q05JY7; -.
DR   PRIDE; Q05JY7; -.
DR   KEGG; ag:BAF35571; -.
DR   BRENDA; 3.2.1.162; 7116.
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:16926183"
FT   CHAIN           26..942
FT                   /note="Lambda-carrageenase"
FT                   /evidence="ECO:0000269|PubMed:16926183"
FT                   /id="PRO_0000398807"
SQ   SEQUENCE   942 AA;  105574 MW;  05C7F34972A18C72 CRC64;
     MKIKILSAMI ASSLLIGCVI PTVKASQSAI KSIETNRTIT KVRTGMLSGG SSIITTSYEG
     TVAAYKFNGE KLWENELSGF MNHDIWVQDI NGDGLVEIFA ANADGNVYCI NSDGSLKWTF
     GLNEVPMNSV TVISDADEKY VVAGGYDKNL YYISANGELL KTIESSAYSE EGVFGDGVKP
     EARTHTVNFV RPVKSSDGTE KLVVLGTNNS LQSSGRFYIF EPFADLPSEK SRISIKKGIG
     DLRTVDFDND GNDELTLGNS AQIGDAAISV MNLDDLSQKK SQINDIARRI DRFGYRVAQT
     EVVMNEGTPT YLTLFGSRIL LTPESFDVND SEILANKYSY YDIWKDKSSN KLVLASAQSG
     GSQVHIIDTS NPSWKSAYEE LEPQGKLAAI QENTREVERQ LSNFQKPTRE RAPLPVYFIS
     ESRNEIPATI ERSESLYDSP VFLNYSTLPN VENWDRSEVL ADNPKYRDKR DRRKNYTLSS
     EEMFNKLSAG YESSDGISQW AGHGNDPYMI SLATMKRIIS SGDGKKTVNI YPEIEGHGDA
     FNKVLNDHFY 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 ANGEQVMAAD SVRYRQIKNK
     IEEKSNLLPM TVSGEAAWVV AQSARKHLRL TLVDSGYLNP SNKVAKVKFN SVTPVAIVDV
     LSGETFSPDS NGVVEIPVLA GAFRFIDVKI TEDLRNMQSS TL
 
 
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