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Database: UniProt
Entry: A0A2S8VUL0_9CAUL
LinkDB: A0A2S8VUL0_9CAUL
Original site: A0A2S8VUL0_9CAUL 
ID   A0A2S8VUL0_9CAUL        Unreviewed;       339 AA.
AC   A0A2S8VUL0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Cysteine synthase A {ECO:0000313|EMBL:PQZ75781.1};
GN   ORFNames=CQ026_14525 {ECO:0000313|EMBL:PQZ75781.1};
OS   Brevundimonas sp. MYb31.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1848616 {ECO:0000313|EMBL:PQZ75781.1, ECO:0000313|Proteomes:UP000238612};
RN   [1] {ECO:0000313|EMBL:PQZ75781.1, ECO:0000313|Proteomes:UP000238612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYb31 {ECO:0000313|EMBL:PQZ75781.1,
RC   ECO:0000313|Proteomes:UP000238612};
RA   Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA   Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA   Kaleta C., Schulenburg H.;
RT   "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT   from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL   Submitted (SEP-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   -!- 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:PQZ75781.1}.
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DR   EMBL; PCPM01000030; PQZ75781.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8VUL0; -.
DR   OrthoDB; 9805733at2; -.
DR   Proteomes; UP000238612; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProt.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF211; CYSTEINE SYNTHASE 1; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          8..305
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   339 AA;  35539 MW;  967C27D67201A18F CRC64;
     MSIASIINLI GDTPLIRLNR LSDATGCEIL GKAEFLNPGQ SIKDRAALSI VQKAKASGAL
     RPGGVIVEGT AGNTGIGLAL VGAALGHRVV IVMPRTQSEE KKLAIRALGA RLIEVDAAPF
     SSPNHFVHYS EEVARKLNAS EPHGALWANQ FDNTANRAAH YEGTAAEIWA QTGGRVDAFV
     SAVGSGGTLA GVGAFLRERK PAVKIALADP AGASLYTWFT LGQMTGEGSS ITEGIGVARI
     TGNLEGFTPD FAYRVEDAEF LPILFDLVTH EGLSLGGSSG VNLAGAVRLA RDIGPGKTIV
     TVLCDPGTRY ASRLFNPTFL RSKGLPTPQW VAEDVRELA
//
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