ID A0A0B8NWT1_9VIBR Unreviewed; 354 AA.
AC A0A0B8NWT1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=cysteine synthase {ECO:0000256|ARBA:ARBA00012681};
DE EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681};
GN ORFNames=JCM19231_3959 {ECO:0000313|EMBL:GAM59000.1};
OS Vibrio ishigakensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1481914 {ECO:0000313|EMBL:GAM59000.1, ECO:0000313|Proteomes:UP000031671};
RN [1] {ECO:0000313|EMBL:GAM59000.1, ECO:0000313|Proteomes:UP000031671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RT "Vibrio sp. C1 JCM 19231 whole genome shotgun sequence.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAM59000.1, ECO:0000313|Proteomes:UP000031671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RG NBRP consortium;
RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RL Submitted (JAN-2015) 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 -!- 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:GAM59000.1}.
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DR EMBL; BBRZ01000117; GAM59000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B8NWT1; -.
DR Proteomes; UP000031671; Unassembled WGS sequence.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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:SF35; MITOCHONDRIAL CYSTEINE SYNTHASE-RELATED; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031671};
KW Transferase {ECO:0000313|EMBL:GAM59000.1}.
FT DOMAIN 16..309
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 354 AA; 38825 MW; 9F2EE55DEF97DB8D CRC64;
MDYGAFMSNT LVANSVSELI GDTDIVRINS LSEISGCEIL LKCEHQNPGG SIKDRAALQL
VTDAIESGKL KPGMTIVEGT AGNTGIGLAL VAKALGYKML VVMPKGQAQE KERMIALHGA
DLLLVDPCPF SNPKHFYHTA KRIGAENEDY WWADQFENLS NYRAHYLNTG PEIWEQTQGK
IDALVSVVGT GGSIAGNSHY LSEKNPNLKT WAIDRWIWDL FLSKSGEYKS SGSSFTEGIG
IMREVENFRQ AKINHAINLP DQDLVTISRL VAEKDGILLG SSSSLNVAGA LYAAARMGKG
NTIVTFSCDL AERSYSKLYN LEFLKEKGIK LDKETLPELW ARYQADGDEK VVNV
//
