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Database: UniProt
Entry: A0A245ZTU2_9SPHN
LinkDB: A0A245ZTU2_9SPHN
Original site: A0A245ZTU2_9SPHN 
ID   A0A245ZTU2_9SPHN        Unreviewed;       336 AA.
AC   A0A245ZTU2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=L-cysteate sulfo-lyase {ECO:0000313|EMBL:OWK33164.1};
DE            EC=4.4.1.25 {ECO:0000313|EMBL:OWK33164.1};
GN   Name=cuyA {ECO:0000313|EMBL:OWK33164.1};
GN   ORFNames=SPDO_00380 {ECO:0000313|EMBL:OWK33164.1};
OS   Sphingomonas dokdonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=344880 {ECO:0000313|EMBL:OWK33164.1, ECO:0000313|Proteomes:UP000197290};
RN   [1] {ECO:0000313|EMBL:OWK33164.1, ECO:0000313|Proteomes:UP000197290}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21029 {ECO:0000313|EMBL:OWK33164.1,
RC   ECO:0000313|Proteomes:UP000197290};
RA   Poehlein A., Wuebbeler J.H., Steinbuechel A., Daniel R.;
RT   "Genome sequence of Sphingomonas dokdonensis DSM 21029.";
RL   Submitted (MAR-2017) 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:OWK33164.1}.
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DR   EMBL; NBBI01000001; OWK33164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A245ZTU2; -.
DR   OrthoDB; 9801249at2; -.
DR   Proteomes; UP000197290; Unassembled WGS sequence.
DR   GO; GO:0034011; F:L-cysteate sulfo-lyase 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:OWK33164.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR006278-2}.
FT   DOMAIN          13..318
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   ACT_SITE        76
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT   MOD_RES         49
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006278-2"
SQ   SEQUENCE   336 AA;  34538 MW;  3C6A84D342F012F8 CRC64;
     MNLAQFARRR YTPGVTAIEP MPHLSRSLGG ATLYIKRDDQ LGLTAGGNKT RKLEFLVADA
     LAQGADTLIT VGAVQSNHCR LTLAAAVREG LKCRLVLEQR VPGSYDPAAS GNNFLFDLLG
     VEAVTVIEAG TDLQAAMEAV AADLAAQGRK GYIIPGGGSN ALGALGYVAC AEEILQQSFE
     MGVAFDRIVV ASGSAGTHAG IVAGIIGNSA GIPVTGVNVR RPRPEQEGNV HKLACAVADL
     AGVVPEVPRD AIVCLDDWVG PGYSIPTPEM VEAVRLFASH EGVLLDPVYT GKAAAGLIGL
     VRSGAIGADE TVLFIHTGGA PALYAYQGIL SGAASA
//
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