YESW_BACSU
ID YESW_BACSU Reviewed; 620 AA.
AC O31526;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Rhamnogalacturonan endolyase YesW;
DE EC=4.2.2.23 {ECO:0000269|PubMed:17449691, ECO:0000269|PubMed:19193638};
DE Flags: Precursor;
GN Name=yesW; OrderedLocusNames=BSU07050;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP PROTEIN SEQUENCE OF 38-46, CRYSTALLIZATION, COFACTOR, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=16682770; DOI=10.1107/s1744309106011894;
RA Ochiai A., Yamasaki M., Itoh T., Mikami B., Hashimoto W., Murata K.;
RT "Crystallization and preliminary X-ray analysis of the rhamnogalacturonan
RT lyase YesW from Bacillus subtilis strain 168, a member of polysaccharide
RT lyase family 11.";
RL Acta Crystallogr. F 62:438-440(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=17449691; DOI=10.1128/aem.00147-07;
RA Ochiai A., Itoh T., Kawamata A., Hashimoto W., Murata K.;
RT "Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene
RT clusters responsible for rhamnogalacturonan depolymerization.";
RL Appl. Environ. Microbiol. 73:3803-3813(2007).
RN [4] {ECO:0007744|PDB:2Z8R, ECO:0007744|PDB:2Z8S}
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 38-620 IN COMPLEX WITH
RP GALACTURONAN DISACCHARIDE AND CALCIUM IONS, AND MUTAGENESIS OF HIS-363;
RP HIS-399; ASP-401; GLU-422; ARG-452; LYS-535 AND TYR-595.
RC STRAIN=168;
RX PubMed=17947240; DOI=10.1074/jbc.m704663200;
RA Ochiai A., Itoh T., Maruyama Y., Kawamata A., Mikami B., Hashimoto W.,
RA Murata K.;
RT "A novel structural fold in polysaccharide lyases: Bacillus subtilis family
RT 11 rhamnogalacturonan lyase YesW with an eight-bladed beta-propeller.";
RL J. Biol. Chem. 282:37134-37145(2007).
RN [5] {ECO:0007744|PDB:2ZUX}
RP X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 38-620 IN COMPLEX WITH CALCIUM
RP AND RHAMNOSE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND DOMAIN.
RC STRAIN=168 {ECO:0000303|PubMed:19193638};
RX PubMed=19193638; DOI=10.1074/jbc.m807799200;
RA Ochiai A., Itoh T., Mikami B., Hashimoto W., Murata K.;
RT "Structural determinants responsible for substrate recognition and mode of
RT action in family 11 polysaccharide lyases.";
RL J. Biol. Chem. 284:10181-10189(2009).
CC -!- FUNCTION: Pectinolytic enzyme that degrades type I rhamnogalacturonan
CC from plant cell walls and releases oligosaccharide products
CC (PubMed:16682770, PubMed:17449691, PubMed:19193638). Degrades
CC rhamnogalacturonan, polygalacturonic acid, pectic acid and pectin
CC (PubMed:16682770, PubMed:17449691). {ECO:0000269|PubMed:16682770,
CC ECO:0000269|PubMed:17449691, ECO:0000269|PubMed:19193638}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-
CC (1->4)-alpha-D-galactopyranosyluronic acid bonds of
CC rhamnogalacturonan I domains in ramified hairy regions of pectin
CC leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-
CC unsaturated D-galactopyranosyluronic acid at the non-reducing end.;
CC EC=4.2.2.23; Evidence={ECO:0000269|PubMed:17449691,
CC ECO:0000269|PubMed:19193638};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:16682770, ECO:0000269|PubMed:17449691,
CC ECO:0000269|PubMed:17947240, ECO:0000269|PubMed:19193638};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16682770, ECO:0000269|PubMed:17449691};
CC Note=Binds 10 calcium ions (PubMed:16682770, PubMed:17449691,
CC PubMed:19193638). The calcium may have a structural role. Requires
CC calcium or manganese for activity (PubMed:16682770, PubMed:17449691).
CC {ECO:0000269|PubMed:16682770, ECO:0000269|PubMed:17449691,
CC ECO:0000269|PubMed:19193638};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.181 mg/ml for rhamnogalacturonan (RG) type I region of plant
CC cell wall pectin {ECO:0000269|PubMed:19193638};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:17449691};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:17449691};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16682770,
CC ECO:0000269|PubMed:17947240, ECO:0000269|PubMed:19193638}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17449691}.
CC -!- INDUCTION: Up-regulated by growth on type I rhamnogalacturonan.
CC {ECO:0000269|PubMed:17449691}.
CC -!- DOMAIN: Rhamnose is bound near the active site, but there are also
CC additional rhamnose-binding sites far away from the active site, which
CC possibly function as a carbohydrate-binding region.
CC {ECO:0000269|PubMed:19193638}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 11 family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB12524.1; -; Genomic_DNA.
DR PIR; F69797; F69797.
DR RefSeq; NP_388586.1; NC_000964.3.
DR RefSeq; WP_010886436.1; NZ_JNCM01000032.1.
DR PDB; 2Z8R; X-ray; 1.40 A; A/B=38-620.
DR PDB; 2Z8S; X-ray; 2.50 A; A/B=38-620.
DR PDB; 2ZUX; X-ray; 1.32 A; A/B=38-620.
DR PDBsum; 2Z8R; -.
DR PDBsum; 2Z8S; -.
DR PDBsum; 2ZUX; -.
DR AlphaFoldDB; O31526; -.
DR SMR; O31526; -.
DR STRING; 224308.BSU07050; -.
DR CAZy; PL11; Polysaccharide Lyase Family 11.
DR PaxDb; O31526; -.
DR PRIDE; O31526; -.
DR EnsemblBacteria; CAB12524; CAB12524; BSU_07050.
DR GeneID; 938769; -.
DR KEGG; bsu:BSU07050; -.
DR PATRIC; fig|224308.43.peg.743; -.
DR eggNOG; COG3401; Bacteria.
DR InParanoid; O31526; -.
DR OMA; TRRWTFD; -.
DR PhylomeDB; O31526; -.
DR BioCyc; BSUB:BSU07050-MON; -.
DR BioCyc; MetaCyc:BSU07050-MON; -.
DR BRENDA; 4.2.2.23; 658.
DR SABIO-RK; O31526; -.
DR EvolutionaryTrace; O31526; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR CDD; cd10318; RGL11; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR041624; RGI_lyase.
DR InterPro; IPR034641; RGL11.
DR PANTHER; PTHR43118; PTHR43118; 1.
DR Pfam; PF18370; RGI_lyase; 1.
DR SUPFAM; SSF69318; SSF69318; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Lyase; Metal-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000305|PubMed:16682770"
FT CHAIN 38..620
FT /note="Rhamnogalacturonan endolyase YesW"
FT /id="PRO_0000360212"
FT REGION 133..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUX"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUX"
FT BINDING 187
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUX"
FT BINDING 207
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUX"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 238
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUX"
FT BINDING 255
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUX"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 369
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 373
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 373
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 375
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="7"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 452
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8S,
FT ECO:0007744|PDB:2ZUX"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8S,
FT ECO:0007744|PDB:2ZUX"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="8"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 496
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="9"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="9"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="9"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="9"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 532..534
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19193638,
FT ECO:0007744|PDB:2ZUX"
FT BINDING 543
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="10"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 545
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="10"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="10"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 549
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="10"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 551
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="10"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 592
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 594
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT BINDING 595
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8S,
FT ECO:0007744|PDB:2ZUX"
FT BINDING 596
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17947240,
FT ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R,
FT ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX"
FT MUTAGEN 363
FT /note="H->A: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:17947240"
FT MUTAGEN 399
FT /note="H->A: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:17947240"
FT MUTAGEN 401
FT /note="D->N: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:17947240"
FT MUTAGEN 422
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17947240"
FT MUTAGEN 452
FT /note="R->A: Strongly reduced catalytic activity and
FT reduced affinity for substrate."
FT /evidence="ECO:0000269|PubMed:17947240"
FT MUTAGEN 535
FT /note="K->A: Strongly reduced catalytic activity and
FT reduced affinity for substrate."
FT /evidence="ECO:0000269|PubMed:17947240"
FT MUTAGEN 595
FT /note="Y->F: Strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:17947240"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 121..132
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:2ZUX"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:2Z8S"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2Z8S"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:2ZUX"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:2ZUX"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:2ZUX"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 340..348
FT /evidence="ECO:0007829|PDB:2ZUX"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:2ZUX"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:2Z8R"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 496..500
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:2ZUX"
FT TURN 514..517
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 518..524
FT /evidence="ECO:0007829|PDB:2ZUX"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 539..542
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 545..549
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 551..556
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 559..565
FT /evidence="ECO:0007829|PDB:2ZUX"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:2ZUX"
FT HELIX 584..590
FT /evidence="ECO:0007829|PDB:2ZUX"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:2ZUX"
SQ SEQUENCE 620 AA; 67587 MW; D4573AF7B3E9358D CRC64;
MRRSCLMIRR RKRMFTAVTL LVLLVMGTSV CPVKAEGAAR QMEALNRGLV AVKTDGGIFV
SWRFLGTENA SVLFNVYRDG QKLNAAPVKT TNYVDKNGSA GSTYTVRAVV NGTEQPASEK
ASVWAQPYHS VPLDKPAGGT TPKGESYTYS ANDASVGDVD GDGQYELILK WDPSNSKDNS
QDGYTGDVLI DAYKLDGTKL WRINLGKNIR AGAHYTQFMV YDLDGDGKAE VAMKTADGTK
DGTGKVIGNA NADYRNEQGR VLSGPEYLTV FQGSTGKELV TANFEPARGN VSDWGDSYGN
RVDRFLAGIA YLDGQRPSLI MTRGYYAKTM LVAYNFRDGK LSKLWTLDSS KSGNEAFAGQ
GNHNLSIADV DGDGKDEIIF GSMAVDHDGK GMYSTGLGHG DALHTGDLDP GRPGLEVFQV
HEDKNAKYGL SFRDAATGKI LWGVYAGKDV GRGMAADIDP RYPGQEVWAN GSLYSAKGVK
IGSGVPSSTN FGIWWDGDLL REQLDSNRID KWDYQNGVSK NMLTASGAAA NNGTKATPTL
QADLLGDWRE EVVWRTEDSS ALRIYTTTIP TEHRLYTLMH DPVYRLGIAW QNIAYNQPPH
TSFFLGDGMA EQPKPNMYTP
