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Database: UniProt
Entry: A0A162TG10_9CLOT
LinkDB: A0A162TG10_9CLOT
Original site: A0A162TG10_9CLOT 
ID   A0A162TG10_9CLOT        Unreviewed;       330 AA.
AC   A0A162TG10;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=D-cysteine desulfhydrase {ECO:0000313|EMBL:KZL92593.1};
DE            EC=4.4.1.15 {ECO:0000313|EMBL:KZL92593.1};
GN   Name=dcyD {ECO:0000313|EMBL:KZL92593.1};
GN   ORFNames=CLMAG_24070 {ECO:0000313|EMBL:KZL92593.1};
OS   Clostridium magnum DSM 2767.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL92593.1, ECO:0000313|Proteomes:UP000076603};
RN   [1] {ECO:0000313|EMBL:KZL92593.1, ECO:0000313|Proteomes:UP000076603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL92593.1,
RC   ECO:0000313|Proteomes:UP000076603};
RA   Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT   "Genome sequence of Clostridium magnum DSM 2767.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC       family. {ECO:0000256|ARBA:ARBA00008639}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZL92593.1}.
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DR   EMBL; LWAE01000002; KZL92593.1; -; Genomic_DNA.
DR   RefSeq; WP_066622169.1; NZ_LWAE01000002.1.
DR   AlphaFoldDB; A0A162TG10; -.
DR   STRING; 1121326.CLMAG_24070; -.
DR   PATRIC; fig|1121326.3.peg.2405; -.
DR   OrthoDB; 9801249at2; -.
DR   Proteomes; UP000076603; Unassembled WGS sequence.
DR   GO; GO:0019148; F:D-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR027278; ACCD_DCysDesulf.
DR   InterPro; IPR005966; D-Cys_desShydrase.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01275; ACC_deam_rel; 1.
DR   PANTHER; PTHR43780; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR   PANTHER; PTHR43780:SF2; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:KZL92593.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR006278-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076603}.
FT   DOMAIN          11..315
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   ACT_SITE        75
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT   MOD_RES         48
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006278-2"
SQ   SEQUENCE   330 AA;  36686 MW;  08CB89039223766E CRC64;
     MIKIPEKINI ANLPTRIEKL EKLSEKLGGP NIYIKRDDQT GMETSGNKVR KLEFSVKEAI
     DRGCDTLITC GGIQSNHCRA TAAIAAKLSL KSCLVLKGSS DEEVDGNLFL DKLLGAEIHF
     ITPEEYKNRR MEIMKEIKSS MEEKGFKPYI IPEGASNGIG GFGYYKTMEE IIDQEKELGV
     HFDGIVVATG SGGTYSGLLL ASKILNHSGR IYGVNVCDDE EYFKSKIHEI LNESINYLNI
     DLSFSKDEIH IMDGYVGKGY ALSRKEELEF ISDFAKMEGI VVDPVYTGKA MYGLTEEIKK
     GSFSECKNLL FIHTGGIFGI FPGKKLFENL
//
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