CCSD_UNKP
ID CCSD_UNKP Reviewed; 359 AA.
AC A0A2I9;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Cysteine/Cysteine sulfinic acid decarboxylase {ECO:0000305};
DE EC=4.1.1.- {ECO:0000269|PubMed:17420004, ECO:0000269|Ref.2};
DE EC=4.1.1.29 {ECO:0000269|PubMed:29796005, ECO:0000269|Ref.3};
DE AltName: Full=Cysteine decarboxylase {ECO:0000303|PubMed:17420004};
DE AltName: Full=L-cysteine sulfinate decarboxylase {ECO:0000303|PubMed:29796005};
DE Short=CSD {ECO:0000303|PubMed:29796005};
DE AltName: Full=Sulfinoalanine decarboxylase {ECO:0000305};
GN Name=undec1A {ECO:0000303|PubMed:17420004};
OS Unknown prokaryotic organism.
OC Bacteria; environmental samples.
OX NCBI_TaxID=2725;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17420004; DOI=10.1016/j.bbrc.2007.03.159;
RA Jiang C., Wu B.;
RT "Molecular cloning and functional characterization of a novel decarboxylase
RT from uncultured microorganisms.";
RL Biochem. Biophys. Res. Commun. 357:421-426(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF HIS-30 AND SER-113.
RX DOI=10.1016/j.enzmictec.2009.03.003;
RA Jiang C., Shen P., Yan B., Wu B.;
RT "Biochemical characterization of a metagenome-derived decarboxylase.";
RL Enzyme Microb. Technol. 45:58-63(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.13343/j.cnki.wsxb.20170133;
RA Deng J., Wu Q., Gao H., Xu Y., Ou Q., Wu B., Jiang C.;
RT "Protein engineering by random mutagenesis and analysis of a metagenome-
RT derived cysteine sulfinate decarboxylase.";
RL Acta Microbiol. Sin. 57:1283-1292(2017).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29796005; DOI=10.17113/ftb.56.01.18.5415;
RA Deng J., Wu Q., Gao H., Ou Q., Wu B., Yan B., Jiang C.;
RT "Molecular characterization and directed evolution of a metagenome-derived
RT L-cysteine sulfinate decarboxylase.";
RL Food Technol. Biotechnol. 56:117-123(2018).
CC -!- FUNCTION: Catalyzes the decarboxylation of L-cysteine to cysteamine and
CC of 3-sulfino-L-alanine (cysteine sulfinic acid) to hypotaurine
CC (PubMed:17420004, Ref.2, Ref.3, PubMed:29796005). Also catalyzes the
CC decarboxylation of various amino acids such as L-lysine, L-glutamate,
CC L-asparaginate and L-proline (Ref.2). In vitro, shows highest activity
CC with L-cysteine as substrate (Ref.2). {ECO:0000269|PubMed:17420004,
CC ECO:0000269|PubMed:29796005, ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-cysteine = CO2 + cysteamine; Xref=Rhea:RHEA:27746,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:58029; Evidence={ECO:0000269|PubMed:17420004,
CC ECO:0000269|Ref.2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-sulfino-L-alanine + H(+) = CO2 + hypotaurine;
CC Xref=Rhea:RHEA:16877, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57853, ChEBI:CHEBI:61085; EC=4.1.1.29;
CC Evidence={ECO:0000269|PubMed:29796005, ECO:0000269|Ref.3};
CC -!- ACTIVITY REGULATION: Slightly stimulated in the presence of 1 mM
CC Mg(2+). {ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.59 mM for L-cysteine {ECO:0000269|Ref.2};
CC KM=1.557 mM for L-cysteine sulfinic acid {ECO:0000269|Ref.3};
CC Note=kcat is 4.57 min(-1) with L-cysteine as substrate (Ref.2). kcat
CC is 45.8 min(-1) with L-cysteine sulfinic acid as substrate (Ref.3).
CC {ECO:0000269|Ref.2, ECO:0000269|Ref.3};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- SIMILARITY: In the N-terminal section; belongs to the HFCD (homo-
CC oligomeric flavin containing Cys decarboxylase) superfamily.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PPC synthetase
CC family. {ECO:0000305}.
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DR EMBL; EF015465; ABJ80896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I9; -.
DR SMR; A0A2I9; -.
DR BRENDA; 4.1.1.29; 12464.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004782; F:sulfinoalanine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0015941; P:pantothenate catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.10300; -; 1.
DR Gene3D; 3.40.50.1950; -; 1.
DR HAMAP; MF_02225; CoaBC; 1.
DR InterPro; IPR035929; CoaB-like_sf.
DR InterPro; IPR005252; CoaBC.
DR InterPro; IPR007085; DNA/pantothenate-metab_flavo_C.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR Pfam; PF04127; DFP; 1.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF102645; SSF102645; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
DR TIGRFAMs; TIGR00521; coaBC_dfp; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Lyase.
FT CHAIN 1..359
FT /note="Cysteine/Cysteine sulfinic acid decarboxylase"
FT /id="PRO_0000445604"
FT MUTAGEN 30
FT /note="H->N: Loss of decarboxylase activity."
FT /evidence="ECO:0000269|Ref.2"
FT MUTAGEN 113
FT /note="S->R: Loss of 80% of decarboxylase activity."
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 359 AA; 38807 MW; 2F98262BE9AB6B6C CRC64;
MITPLTLATL SKNPILVDFF DPEDGRWNSH VDLGLWSDLY LIAPATANTI GKMAAGIADN
LLLTSYLSAR CPVFIAPAMD VDMLMHPATQ RNLGILKSSG NHIIEPGSGE LASGLTGKGR
MAEPEEIVRE VISFFSKKKI TEKPLNGRRV FINAGPTIEP IDPVRFISNY SSGRMGIALA
DAAAAMGAEV TLVLGPVTLR PSSQDINVID VRSAAEMKEA SVEAFRECDI AILAAAVADF
TPLTTSDKKI KRGSGEMVIN LRPTEDIAAE LGKMKKKNQL LVGFALETDD EITNASSKLK
RKNLDMIVLN SLKDPGAGFG HETNRITIID KSNNIDKFEL KTKGEVAADI IRKILTLVH
