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Database: UniProt
Entry: A0A1I3RZ69_9BRAD
LinkDB: A0A1I3RZ69_9BRAD
Original site: A0A1I3RZ69_9BRAD 
ID   A0A1I3RZ69_9BRAD        Unreviewed;       325 AA.
AC   A0A1I3RZ69;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Cysteine synthase {ECO:0000256|ARBA:ARBA00012681, ECO:0000256|RuleBase:RU003985};
DE            EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681, ECO:0000256|RuleBase:RU003985};
GN   ORFNames=SAMN05216525_12721 {ECO:0000313|EMBL:SFJ51618.1};
OS   Bradyrhizobium sp. Gha.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1855318 {ECO:0000313|EMBL:SFJ51618.1, ECO:0000313|Proteomes:UP000199284};
RN   [1] {ECO:0000313|EMBL:SFJ51618.1, ECO:0000313|Proteomes:UP000199284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gha {ECO:0000313|EMBL:SFJ51618.1,
RC   ECO:0000313|Proteomes:UP000199284};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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         ECO:0000256|RuleBase:RU003985};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR605856-50, ECO:0000256|RuleBase:RU003985};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004895}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000256|ARBA:ARBA00007103,
CC       ECO:0000256|RuleBase:RU003985}.
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DR   EMBL; FOQM01000027; SFJ51618.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3RZ69; -.
DR   STRING; 1855318.SAMN05216525_12721; -.
DR   OrthoDB; 9805733at2; -.
DR   UniPathway; UPA00136; UER00200.
DR   Proteomes; UP000199284; Unassembled WGS sequence.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR005856; Cys_synth.
DR   InterPro; IPR005859; CysK.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01139; cysK; 1.
DR   NCBIfam; TIGR01136; cysKM; 1.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF253; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003985};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192,
KW   ECO:0000256|RuleBase:RU003985};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR605856-50};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT   DOMAIN          25..310
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         91
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         195..199
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         283
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         61
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   325 AA;  34208 MW;  E0A053C1E244A44A CRC64;
     MDASSNTGAA HQPGRGRIYS SIVEAFGDTP IVRLRRLPGM HGVNATILAK LEYFNPAASV
     KDRIGAAMII AMEKAGIIKP DTVLIEPTSG NTGIALAYVA ASRGYRLKLV MPESMSIERR
     KMLAFLGAEL VLTPAAQGMK GAIAAAEELL KTTPNSVMPQ QFKNLANPEV HRRTTAEEIW
     NDTSGNIDFF VAGVGTGGTI TGVGQVLKPR KASLRVVAVE PEESPVLSGG QHTPHKIQGI
     GAGFVPDILD RSVIDEIVKI NSTTAIETSR ALARHEGIPG GISAGAAIAA ALEIGKRPEA
     AGKTILAIVP SFSERYLSTV LFEGI
//
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