ID   PLH29_FORAG             Reviewed;         638 AA.
AC   T2KMH5;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 2.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Broad-specificity ulvan lyase {ECO:0000303|PubMed:30279430};
DE            EC=4.2.2.- {ECO:0000269|PubMed:30279430};
DE            EC=4.2.2.20 {ECO:0000269|PubMed:30279430};
DE            EC=4.2.2.8 {ECO:0000269|PubMed:30279430};
DE   AltName: Full=P29 {ECO:0000303|PubMed:31285597};
DE   AltName: Full=Polysaccharide utilization locus H protein P29 {ECO:0000303|PubMed:31285597};
DE            Short=PUL H protein P29;
DE   Flags: Precursor;
GN   ORFNames=BN863_22180;
OS   Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS   M-2Alg 35-1).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Formosa.
OX   NCBI_TaxID=1347342;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1;
RX   PubMed=23995932; DOI=10.1128/aem.01937-13;
RA   Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA   Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA   Amann R.I., Teeling H.;
RT   "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT   KMM 3901T reveals a broad potential for degradation of algal
RT   polysaccharides.";
RL   Appl. Environ. Microbiol. 79:6813-6822(2013).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   DOI=10.1016/j.algal.2017.09.025;
RA   Salinas A., French C.E.;
RT   "The enzymatic ulvan depolymerisation system from the alga-associated
RT   marine flavobacterium Formosa agariphila.";
RL   Algal Res. 27:335-344(2017).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=30279430; DOI=10.1038/s41598-018-32922-0;
RA   Konasani V.R., Jin C., Karlsson N.G., Albers E.;
RT   "A novel ulvan lyase family with broad-spectrum activity from the ulvan
RT   utilisation loci of Formosa agariphila KMM 3901.";
RL   Sci. Rep. 8:14713-14713(2018).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=31285597; DOI=10.1038/s41589-019-0311-9;
RA   Reisky L., Prechoux A., Zuehlke M.K., Baeumgen M., Robb C.S., Gerlach N.,
RA   Roret T., Stanetty C., Larocque R., Michel G., Song T., Markert S.,
RA   Unfried F., Mihovilovic M.D., Trautwein-Schult A., Becher D., Schweder T.,
RA   Bornscheuer U.T., Hehemann J.H.;
RT   "A marine bacterial enzymatic cascade degrades the algal polysaccharide
RT   ulvan.";
RL   Nat. Chem. Biol. 15:803-812(2019).
CC   -!- FUNCTION: Broad-specificity lyase involved in ulvan degradation
CC       (PubMed:30279430). Ulvan is the main polysaccharide component of the
CC       Ulvales (green seaweed) cell wall. It is composed of disaccharide
CC       building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-
CC       glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl)
CC       (PubMed:30279430) (Probable). Ulvan lyase catalyzes the endolytic
CC       cleavage of the glycosidic bond between Rha3S and the uronic acids GlcA
CC       or IduA, producing oligosaccharides that have unsaturated 4-deoxy-L-
CC       threo-hex-4-enopyranosiduronic acid (deltaUA) at the non-reducing end.
CC       This results eventually in the degradation of the ulvan polysaccharide
CC       into deltaUA-Rha3S disaccharides and deltaUA-Rha3S-Xyl-Rha3S
CC       tetrasaccharides. It is also able to degrade the glycosaminoglycans
CC       heparan sulfate and chondroitin sulfate. Not active against pectin,
CC       xanthan or alginate (PubMed:30279430). {ECO:0000269|PubMed:30279430,
CC       ECO:0000305|PubMed:31285597}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endolytic cleavage of (1->4)-beta-galactosaminic bonds between
CC         N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid
CC         to produce a mixture of Delta(4)-unsaturated oligosaccharides of
CC         different sizes that are ultimately degraded to Delta(4)-unsaturated
CC         tetra- and disaccharides.; EC=4.2.2.20;
CC         Evidence={ECO:0000269|PubMed:30279430};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Elimination of sulfate, appears to act on linkages between N-
CC         acetyl-D-glucosamine and uronate. Product is an unsaturated sugar.;
CC         EC=4.2.2.8; Evidence={ECO:0000269|PubMed:30279430};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.77 mg/ml for ulvan {ECO:0000269|PubMed:30279430};
CC       pH dependence:
CC         Optimum pH is 8. {ECO:0000269|PubMed:30279430};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:30279430};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:30279430,
CC       ECO:0000305|PubMed:31285597}.
CC   -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 37 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CDF79930.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|Ref.2};
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DR   EMBL; HG315671; CDF79930.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_038530528.1; NZ_HG315671.1.
DR   AlphaFoldDB; T2KMH5; -.
DR   EnsemblBacteria; CDF79930; CDF79930; BN863_22180.
DR   PATRIC; fig|1347342.6.peg.2225; -.
DR   eggNOG; ENOG502ZAAD; Bacteria.
DR   HOGENOM; CLU_455455_0_0_10; -.
DR   Proteomes; UP000016160; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0034000; F:chondroitin-sulfate-ABC endolyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015021; F:heparin-sulfate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Lyase; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..638
FT                   /note="Broad-specificity ulvan lyase"
FT                   /id="PRO_0000448331"
SQ   SEQUENCE   638 AA;  71117 MW;  A8817A02A81BCBE7 CRC64;
     MKRRNFIQLS SLATIGMSLP SAGIVNACSS FPEQSLEFKN LTSELLKEWC DGMLKVQINN
     PSNLEEHGAL RCPSCSHIHG RCMDAVYPFL YMADVSGDEK YIEAAKLVMI WAENNVSQEN
     GAWTVIPNPK SWKGITIFGA IALAESLHYH SHILDDKTLK AWTNRLARAG QYIYDTFTID
     FTNINYGGTA IYGLDIIGDV LGNGNFKEKS KKMAEEVQAF FTKNDYLLYG ECKPEADKLS
     AKGLHGVDLG YNVEETLNSL VMYALKNDDQ ALLQIVTKSL NSHLEFMLPD GGWDNSWGNR
     MYKWTYWGSR TCDGSQPAFA MMAHINPAFG TAAVKNTELL KQCTANGLLH GGPHYISAGI
     PPCVHHTFTH AKPLAALLDH WKHLPEINKT TALPRVTANG IKHFKDLDVL LFSRGDWRGT
     VSAYDAEYHY KKDYRQATGG SLGILYHNKV GLLCAASMAV YNMVEPYNQQ PQPGKDIALT
     PRIETFKEDQ WYTNLYDLTA NLEAIDTKEV INLASVVKLK NESRKMVSGT ASEFHLTYSC
     AKEGLTIKVS TQQDILEPTA FVLPIASPEK EKVEFVNEHE IKISKPGGVV TIKANVPLKL
     KEYSGTRTFN MVPGLEALPI ELFFETHIKE LVLIVSVV