ID E6WBI4_PANSA Unreviewed; 328 AA.
AC E6WBI4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=D-cysteine desulfhydrase {ECO:0000256|HAMAP-Rule:MF_01045};
DE EC=4.4.1.15 {ECO:0000256|HAMAP-Rule:MF_01045};
GN Name=dcyD {ECO:0000256|HAMAP-Rule:MF_01045};
GN OrderedLocusNames=Pat9b_2367 {ECO:0000313|EMBL:ADU69669.1};
OS Pantoea sp. (strain At-9b).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU69669.1, ECO:0000313|Proteomes:UP000001624};
RN [1] {ECO:0000313|EMBL:ADU69669.1, ECO:0000313|Proteomes:UP000001624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=At-9b {ECO:0000313|EMBL:ADU69669.1,
RC ECO:0000313|Proteomes:UP000001624};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT "Complete sequence chromosome of Pantoea sp. At-9b.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the alpha,beta-elimination reaction of D-cysteine
CC and of several D-cysteine derivatives. It could be a defense mechanism
CC against D-cysteine. {ECO:0000256|HAMAP-Rule:MF_01045}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-cysteine + H2O = H(+) + hydrogen sulfide + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:11268, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:35236; EC=4.4.1.15; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01045};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01045};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01045}.
CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000256|ARBA:ARBA00008639, ECO:0000256|HAMAP-
CC Rule:MF_01045}.
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DR EMBL; CP002433; ADU69669.1; -; Genomic_DNA.
DR RefSeq; WP_013509524.1; NC_014837.1.
DR AlphaFoldDB; E6WBI4; -.
DR STRING; 592316.Pat9b_2367; -.
DR KEGG; pao:Pat9b_2367; -.
DR eggNOG; COG2515; Bacteria.
DR HOGENOM; CLU_048897_1_0_6; -.
DR OrthoDB; 9801249at2; -.
DR Proteomes; UP000001624; Chromosome.
DR GO; GO:0019148; F:D-cysteine desulfhydrase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_01045; D_Cys_desulfhydr; 1.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR005966; D-Cys_desShydrase.
DR InterPro; IPR023702; D_Cys_desulphydr_bac.
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:0000256|HAMAP-Rule:MF_01045};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01045}.
FT DOMAIN 14..316
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01045,
FT ECO:0000256|PIRSR:PIRSR006278-2"
SQ SEQUENCE 328 AA; 35180 MW; 26547CE16CCEAE2C CRC64;
MSLHLLHQFP RLELLGAPTP LEHLPRLSDY LGRDIFIKRD DFTPVALGGN KLRKLEFLAA
DALREGADVL LTAGAIQSNH VRQTAAVAAR LGLKCVALLE NPIGTDAPNY LSNGNRLLLD
LMDVEVVMVA ALHNPAAQLA EQAERLEAQG FRPYVVPVGG SNALGALGYV ECAQEIAHQS
EGVVDFAAVV VASGSAGTHA GLAIGLEQLL PDSELVGVTV SRKVADQLPV VERIRTALAQ
QLEVEAHAPI TLWDDYFAPR YGEPNEEGME AVKLLARLEG IMLDPVYTGK AMAGLIDGVS
QQRFRREGPL LFVHTGGSPA LFAYHPSV
//
