SDC_CUTMO
ID SDC_CUTMO Reviewed; 350 AA.
AC P0CT50;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Salicylate decarboxylase {ECO:0000303|PubMed:20188702};
DE EC=4.1.1.91 {ECO:0000269|PubMed:20188702};
DE AltName: Full=Salicylic acid decarboxylase {ECO:0000303|PubMed:20188702};
GN Name=sdc {ECO:0000303|PubMed:20188702};
OS Cutaneotrichosporon moniliiforme (Yeast) (Trichosporon moniliiforme).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=1895941;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-31 AND 54-64,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC STRAIN=WU-0401;
RX PubMed=20188702; DOI=10.1016/j.bbrc.2010.02.154;
RA Kirimura K., Gunji H., Wakayama R., Hattori T., Ishii Y.;
RT "Enzymatic Kolbe-Schmitt reaction to form salicylic acid from phenol:
RT enzymatic characterization and gene identification of a novel enzyme,
RT Trichosporon moniliiforme salicylic acid decarboxylase.";
RL Biochem. Biophys. Res. Commun. 394:279-284(2010).
CC -!- FUNCTION: Reversibly catalyzes the regioselective carboxylation of
CC phenol to form salicylic acid. Involved in a pathway for the
CC degradation of salicylate via phenol. Also catalyzes the
CC decarboxylation of beta-resorcylic acid (2,4-dihydroxybenzoic acid)
CC into resorcinol (1,3-dihydroxybenzene), gamma-resorcylic acid (2,6-
CC dihydroxybenzoic acid) into resorcinol, 2,3-dihydroxybenzoic acid into
CC catechol (1,2-dihydroxybenzene), and 4-aminosalicylic acid into 3-
CC aminophenol. {ECO:0000269|PubMed:20188702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + salicylate = CO2 + phenol; Xref=Rhea:RHEA:30703,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15882, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30762; EC=4.1.1.91;
CC Evidence={ECO:0000269|PubMed:20188702};
CC -!- ACTIVITY REGULATION: Inhibited by AgNO(3), HgCl(2), p-
CC chloromercuribenzoic acid and NiCl(2). {ECO:0000269|PubMed:20188702}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.08 mM for salicylate (at 40 degrees Celsius and pH 5.5)
CC {ECO:0000269|PubMed:20188702};
CC KM=123 mM for phenol (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:20188702};
CC Vmax=12.2 umol/min/mg enzyme for the decarboxylase activity (at 40
CC degrees Celsius and pH 5.5) {ECO:0000269|PubMed:20188702};
CC Vmax=12.3 umol/min/mg enzyme for the carboxylase activity (at 30
CC degrees Celsius) {ECO:0000269|PubMed:20188702};
CC pH dependence:
CC Optimum pH is 5.5 for decarboxylase activity.
CC {ECO:0000269|PubMed:20188702};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius for the decarboxylase
CC activity and 30 degrees Celsius for carboxylase activity.
CC {ECO:0000269|PubMed:20188702};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20188702}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC {ECO:0000305}.
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DR EMBL; DM040453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 6JQW; X-ray; 1.44 A; A/B=1-350.
DR PDB; 6JQX; X-ray; 1.67 A; A/B=1-350.
DR PDBsum; 6JQW; -.
DR PDBsum; 6JQX; -.
DR AlphaFoldDB; P0CT50; -.
DR SMR; P0CT50; -.
DR BRENDA; 4.1.1.91; 12167.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR InterPro; IPR032465; ACMSD.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR21240; PTHR21240; 1.
DR Pfam; PF04909; Amidohydro_2; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Direct protein sequencing; Lyase.
FT CHAIN 1..350
FT /note="Salicylate decarboxylase"
FT /id="PRO_0000431293"
FT CONFLICT 22
FT /note="E -> V (in Ref. 1; AA sequence)"
FT CONFLICT 54
FT /note="H -> V (in Ref. 1; AA sequence)"
FT CONFLICT 62
FT /note="S -> L (in Ref. 1; AA sequence)"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:6JQW"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 74..92
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:6JQW"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:6JQW"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 110..124
FT /evidence="ECO:0007829|PDB:6JQW"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6JQW"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:6JQW"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:6JQW"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:6JQW"
FT TURN 189..193
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:6JQW"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6JQW"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:6JQW"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:6JQW"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:6JQW"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:6JQW"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:6JQW"
SQ SEQUENCE 350 AA; 39961 MW; A83205AC4BFE7144 CRC64;
MRGKVSLEEA FELPKFAAQT KEKAELYIAP NNRDRYFEEI LNPCGNRLEL SNKHGIGYTI
YSIYSPGPQG WTERAECEEY ARECNDYISG EIANHKDRMG AFAALSMHDP KQASEELTRC
VKELGFLGAL VNDVQHAGPE GETHIFYDQP EWDIFWQTCV DLDVPFYLHP EPPFGSYLRN
QYEGRKYLIG PPVSFANGVS LHVLGMIVNG VFDRFPKLKV ILGHLGEHIP GDFWRIEHWF
EHCSRPLAKS RGDVFAEKPL LHYFRNNIWL TTSGNFSTET LKFCVEHVGA ERILFSVDSP
YEHIDVGCGW YDDNAKAIME AVGGEKAYKD IGRDNAKKLF KLGKFYDSEA
