ID S6I5L5_9PSED Unreviewed; 457 AA.
AC S6I5L5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=cysteine synthase {ECO:0000256|ARBA:ARBA00012681};
DE EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681};
GN ORFNames=CFII64_19648 {ECO:0000313|EMBL:EPJ80103.1};
OS Pseudomonas sp. CFII64.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=911242 {ECO:0000313|EMBL:EPJ80103.1, ECO:0000313|Proteomes:UP000014850};
RN [1] {ECO:0000313|EMBL:EPJ80103.1, ECO:0000313|Proteomes:UP000014850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFII64 {ECO:0000313|EMBL:EPJ80103.1,
RC ECO:0000313|Proteomes:UP000014850};
RA Feris K.P., Lalor S.J.;
RL Submitted (NOV-2010) 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:EPJ80103.1}.
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DR EMBL; ATLO01000042; EPJ80103.1; -; Genomic_DNA.
DR RefSeq; WP_020292528.1; NZ_ATLO01000042.1.
DR AlphaFoldDB; S6I5L5; -.
DR PATRIC; fig|911242.4.peg.3907; -.
DR OrthoDB; 9805733at2; -.
DR Proteomes; UP000014850; 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; 1.
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 Lyase {ECO:0000313|EMBL:EPJ80103.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 337..400
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 457 AA; 49429 MW; 69AAA089FD6B1B9D CRC64;
MPDDSRPAVL GLIGNTPLVR VTRFDTGLCT LFLKLESQNP GGSIKDRIGL AMIDAAERDG
RLRPGGTIVE ATAGNTGLGL ALVGRAKGYR VVLVVPDKMS TEKVLHLKAM GAEVHITRSD
VGKGHHEYYQ DVAARLAQEI PDAFFADQFN NPANPLAHEC STAPEIWAQT EHDLDAIVVG
VGSAGTLTGL TRFFRRVQPD LAMVLADPVG SVMADYSRGQ PLPTPGSWAV EGIGEDFIPS
IADLSSVRQA YSISDEESFD HARQLLRAEG ILGGSSTGTL LAAALRYCRE QTVPKRVVSF
VCDTGTRYLS KVYNDQWMTD QGLLQRTRYG DLRDLIARRF EDGRVISVGP DDTLLTAFQR
MRLADVSQLP VLVDGQRLVG VIDESDILLG VHEDPAHLRL TVASAMTVTL EVLPPGASLV
ELQGKLDRGL VAIIADAAGF HGLITRVDLL NHLRRSL
//
