PLH36_FORAG
ID PLH36_FORAG Reviewed; 1174 AA.
AC T2KM26;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 2.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Bifunctional sulfatase/alpha-L-rhamnosidase {ECO:0000305};
DE AltName: Full=P36_GH78/S1_25 {ECO:0000303|PubMed:31285597};
DE Includes:
DE RecName: Full=Ulvan-active sulfatase;
DE EC=3.1.6.- {ECO:0000269|PubMed:31285597};
DE AltName: Full=Sulfatase family S1 subfamily 25 protein P36 {ECO:0000305};
DE Short=P36_S1_25 {ECO:0000303|PubMed:31285597};
DE Includes:
DE RecName: Full=Alpha-L-rhamnosidase;
DE EC=3.2.1.40 {ECO:0000250|UniProtKB:T2KNB2};
DE AltName: Full=Glycosyl hydrolase 78 family protein P36 {ECO:0000305};
DE Short=P36_GH78 {ECO:0000303|PubMed:31285597};
DE AltName: Full=Polysaccharide utilization locus H protein P36 {ECO:0000303|PubMed:31285597};
DE Short=PUL H protein P36;
DE Flags: Precursor;
GN ORFNames=BN863_22250;
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 X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 28-463 IN COMPLEX WITH CALCIUM
RP ION, 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: Bifunctional enzyme containing sulfatase and alpha-L-
CC rhamnosidase activities involved in ulvan degradation
CC (PubMed:31285597). 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 (Probable). The sulfatase specifically desulfates L-rhamnose at the 3-
CC position and can act on the motif Rha3S-Xyl-Rha3S in an exolytic mode
CC of action, producing Rha-Xyl-Rha3S. Also desulfates Rha3S
CC monosaccharides, which are produced by the action of unsaturated
CC glucuronyl hydrolases acting on ulvan oligomers (PubMed:31285597).
CC {ECO:0000269|PubMed:31285597, ECO:0000305|PubMed:31285597}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-rhamnose residues
CC in alpha-L-rhamnosides.; EC=3.2.1.40;
CC Evidence={ECO:0000250|UniProtKB:T2KNB2};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:31285597};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:31285597};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:31285597}.
CC -!- INDUCTION: By ulvan and rhamnose. {ECO:0000269|PubMed:31285597}.
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity. This post-
CC translational modification is severely defective in multiple sulfatase
CC deficiency (MSD). {ECO:0000250|UniProtKB:P15289}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the sulfatase family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC hydrolase 78 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CDF79937.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|Ref.2};
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DR EMBL; HG315671; CDF79937.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_038530548.1; NZ_HG315671.1.
DR PDB; 6HR5; X-ray; 2.91 A; A=28-463.
DR PDBsum; 6HR5; -.
DR AlphaFoldDB; T2KM26; -.
DR SMR; T2KM26; -.
DR STRING; 1347342.BN863_22250; -.
DR EnsemblBacteria; CDF79937; CDF79937; BN863_22250.
DR PATRIC; fig|1347342.6.peg.2232; -.
DR eggNOG; COG3119; Bacteria.
DR eggNOG; COG3408; Bacteria.
DR HOGENOM; CLU_270303_0_0_10; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0030596; F:alpha-L-rhamnosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR035396; Bac_rhamnosid6H.
DR InterPro; IPR035398; Bac_rhamnosid_C.
DR InterPro; IPR032506; DUF4976.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008902; Rhamnosid_concanavalin.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF05592; Bac_rhamnosid; 1.
DR Pfam; PF17389; Bac_rhamnosid6H; 1.
DR Pfam; PF17390; Bac_rhamnosid_C; 1.
DR Pfam; PF16347; DUF4976; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Hydrolase; Metal-binding; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1174
FT /note="Bifunctional sulfatase/alpha-L-rhamnosidase"
FT /id="PRO_0000448339"
FT REGION 22..568
FT /note="Ulvan-active sulfatase"
FT REGION 569..1174
FT /note="Alpha-L-rhamnosidase"
FT ACT_SITE 78
FT /note="Nucleophile; for sulfatase activity"
FT /evidence="ECO:0000250|UniProtKB:P51691"
FT ACT_SITE 766
FT /note="Proton donor; for alpha-L-rhamnosidase activity"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT ACT_SITE 1044
FT /note="Proton acceptor; for alpha-L-rhamnosidase activity"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:31285597"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:31285597"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P51691"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:31285597"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:31285597"
FT BINDING 764..766
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT BINDING 1058
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0000250|UniProtKB:Q82PP4"
FT MOD_RES 78
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P51691"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 112..117
FT /evidence="ECO:0007829|PDB:6HR5"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 266..290
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:6HR5"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 350..358
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:6HR5"
FT TURN 382..385
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 402..407
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:6HR5"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:6HR5"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:6HR5"
FT HELIX 444..458
FT /evidence="ECO:0007829|PDB:6HR5"
FT TURN 459..461
FT /evidence="ECO:0007829|PDB:6HR5"
SQ SEQUENCE 1174 AA; 134503 MW; AF4C49970929AB52 CRC64;
MIKYKAIINL VFIAVFFNNA MSQTVKKEKP NIIFILTDDQ RFDAIGYAGN KFVNTPEMDK
LAQQGTYFDH AIVTTPICAA SRASLWTGLH ERSHNFNFQT GNVREEYMNN AYPKLLKNNG
YYTGFYGKYG VRYDNLESQF DEFESYDRNN RYKDKRGYYY KTINNDTVHL TRYTGQQAID
FIDKNATNTQ PFMLSLSFSA PHAHDGAPEQ YFWQTTTDAL LQDTTLPGPD LADEKYFLAQ
PQAVRDGFNR LRWTWRYDDP EKYQHSLKGY YRMISGIDLE IKKIRDKLKE KGVDKNTVII
VMGDNGYFLG ERQLAGKWLM YDNSIRVPLI VFDPRVNKHQ DISEMVLNID VTQTIADLAG
VKAPESWQGK SLLPLVKQET STISRDTILI EHLWDFENIP PSEGVRTEEW KYFRYVNDKT
IEELYNIKKD PKEINNLIGK KKYQNVAKAL REKLDELIAK NSDEFRAGPS DLTVELIRQP
ESEVKIFDLK PEFGWTVPLS SKYQSAYQLL VASSETIINA NNGDVWDSGQ VRSSQSTNVD
FGGKPLKIGE TYYWKVRIWD EENRLVDYSK AQKFTIGESD NYIISTENKF VTDKIKPSKF
ENRDGVYFID FGKAAFATME FNYQAKTPHT LTIRVGEMID ENGNVNRTPP AKSNIRYQEL
KVEVKPGQTR YRIPIQTDER NTRPNKAIPL PKGFPPLLPF RYAEIEGAQS SINANDVEQL
AYHTFWDEKA SSFKSDNNIL NQVWDLSKYS IKATTFNGLY VDGDRERIPY EADAYLNQLS
HYTTDREYAM ARRTIEYFMK NPTWPTEWQQ HVALLLYADY MYTGNTELVE RYYEALKHKS
LYELSNEDGL ITSTKVDAEF MKKLGFPEGY KKPLTDIVDW PGANFNGSKT PGERDGFVFQ
PYNTVINSFF YENMKIMAQF AKILGKTDEV LDFELRAAKA KKAVNEQMFD KKRGIYVDGI
GTDHASLHAN MMPLAFGLVP QEHVDTVVEF VKSRGMACSV YGAQFLLDGL YNVGEADYAL
DLLASTSERS WYNMIRIGST ITLEAWDNKY KNNLDWNHAW GAVPANAIPR GLWGIKPKTA
GFGIASIKPQ MGKLKSSQIT VPTVRGAIHA TFTHNGPRSQ TYEIEIPGNM VAEFSLDDID
GKDLIHNGQK VPAAFGAVQL SPGKHIIELK INSF
