ID   F7S0A9_9GAMM            Unreviewed;       321 AA.
AC   F7S0A9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=cysteine synthase {ECO:0000256|ARBA:ARBA00012681};
DE            EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681};
GN   ORFNames=A28LD_1953 {ECO:0000313|EMBL:EGN74459.1};
OS   Idiomarina sp. A28L.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=1036674 {ECO:0000313|EMBL:EGN74459.1, ECO:0000313|Proteomes:UP000053031};
RN   [1] {ECO:0000313|EMBL:EGN74459.1, ECO:0000313|Proteomes:UP000053031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A28L {ECO:0000313|EMBL:EGN74459.1,
RC   ECO:0000313|Proteomes:UP000053031};
RX   PubMed=21742887; DOI=10.1128/JB.05648-11;
RA   Gupta H.K., Singh A., Sharma R.;
RT   "Genome Sequence of Idiomarina sp. Strain A28L, Isolated from Pangong Lake,
RT   India.";
RL   J. Bacteriol. 193:5875-5876(2011).
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:EGN74459.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AFPO01000024; EGN74459.1; -; Genomic_DNA.
DR   RefSeq; WP_007420915.1; NZ_AFPO01000024.1.
DR   AlphaFoldDB; F7S0A9; -.
DR   STRING; 1036674.A28LD_1953; -.
DR   PATRIC; fig|1036674.4.peg.1947; -.
DR   eggNOG; COG0031; Bacteria.
DR   OrthoDB; 9805733at2; -.
DR   Proteomes; UP000053031; Unassembled WGS sequence.
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; 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; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053031}.
FT   DOMAIN          10..300
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   321 AA;  34991 MW;  A1310D3807D7AA83 CRC64;
     MKVYNNALEM IGNTPMVRVN HIDTGPCELY LKLETQNPGA SIKDRIAVTM IAAAEEQGKI
     KPGDTLIEAT AGNTGLGLAL VAAQKGYKLI IVLPDKMSRE KLYNLRALGA EVIETRSDVQ
     KGHPEYYQDL ALRLSKERNA FYINQFENPA NVQAHYETTA PEIWQQMEGN LDAFVCGVGS
     GGTLTGVGRY LREQKADIDL VLADPDGSIL APLINEGKEV EAGSWRVEGI GEDFIPVICE
     IALAGKAYSI SDKESFATAR EVLLKEGIMV GSSSGTLIAA ALQYCREQTE PKRVVTLACD
     TGCRYLSKLF NDEWLAAQDL S
//