ID A0A0A0EXV2_9GAMM Unreviewed; 458 AA.
AC A0A0A0EXV2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=cysteine synthase {ECO:0000256|ARBA:ARBA00012681};
DE EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681};
GN ORFNames=N800_00330 {ECO:0000313|EMBL:KGM55110.1};
OS Lysobacter daejeonensis GH1-9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1385517 {ECO:0000313|EMBL:KGM55110.1, ECO:0000313|Proteomes:UP000029998};
RN [1] {ECO:0000313|EMBL:KGM55110.1, ECO:0000313|Proteomes:UP000029998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GH1-9 {ECO:0000313|EMBL:KGM55110.1,
RC ECO:0000313|Proteomes:UP000029998};
RA Zhang S., Wang G.;
RT "Genome sequencing of Lysobacter.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC Evidence={ECO:0000256|ARBA:ARBA00000298};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2. {ECO:0000256|ARBA:ARBA00004962}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103}.
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:KGM55110.1}.
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DR EMBL; AVPU01000007; KGM55110.1; -; Genomic_DNA.
DR RefSeq; WP_036135883.1; NZ_AVPU01000007.1.
DR AlphaFoldDB; A0A0A0EXV2; -.
DR STRING; 1385517.N800_00330; -.
DR eggNOG; COG0031; Bacteria.
DR eggNOG; COG0517; Bacteria.
DR OrthoDB; 9805733at2; -.
DR Proteomes; UP000029998; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 CDD; cd04608; CBS_pair_CBS; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR046353; CBS_C.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF191; CYSTATHIONINE BETA-SYNTHASE; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00291; PALP; 1.
DR SMART; SM00116; CBS; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000029998}.
FT DOMAIN 341..398
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 458 AA; 50267 MW; 167116C93AC4D660 CRC64;
MSIHASVLEL IGQTPIVKAR NLDTGVCELY FKLESQNPGG SIKDRIGLKM IEAAEARGDI
KPGDTLVEGT AGNTGIGLAL VAQQKGYKLI LVVPDKMSRE KIFNLKAMGA QVVLTRSDVA
KGHPDYYQDM AERIARETPG AYFINQFGNP DNPAAHEFGT GPEILAQMAE VGGLDAIVFG
CGSSGTMTGL SRCFAAHSPQ TELILADPVG SILEEYINRG TLSDKSASWM VEGIGEDFLP
PISDFTRVKK AYAISDKESF LTARMLLERE GILGGSSTGT LLAAALKYCQ EQATPKKVLV
FVCDTGNKYL SKMYNDYWML DNGFLAREPY NDLRDLILRP FSQRDTVVVG PNDLLVTAYQ
RMKLYDVSQL PVMEGDQLVG IVDESDVLLH VYGDESRFRD PVSTAMVSKL DKVDVRAPIE
ALLPVFDRGH VAIVTEGEKF LGLITRIDLL NYLRRRVQ
//
