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
//