ID A0A0G3X6Y2_9SPHN Unreviewed; 306 AA.
AC A0A0G3X6Y2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=AM2010_874 {ECO:0000313|EMBL:AKM06952.1};
OS Pelagerythrobacter marensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Pelagerythrobacter.
OX NCBI_TaxID=543877 {ECO:0000313|EMBL:AKM06952.1, ECO:0000313|Proteomes:UP000037643};
RN [1] {ECO:0000313|EMBL:AKM06952.1, ECO:0000313|Proteomes:UP000037643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22370 {ECO:0000313|EMBL:AKM06952.1,
RC ECO:0000313|Proteomes:UP000037643};
RA Kim K.M.;
RL Submitted (JUN-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 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:PIRSR605856-51, 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; CP011805; AKM06952.1; -; Genomic_DNA.
DR RefSeq; WP_047806044.1; NZ_LMVG01000001.1.
DR AlphaFoldDB; A0A0G3X6Y2; -.
DR STRING; 543877.AM2010_874; -.
DR KEGG; amx:AM2010_874; -.
DR PATRIC; fig|543877.4.peg.883; -.
DR OrthoDB; 9805733at2; -.
DR UniPathway; UPA00136; UER00200.
DR Proteomes; UP000037643; Chromosome.
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:SF194; 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 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:PIRSR605856-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000037643};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT DOMAIN 7..286
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 41
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 306 AA; 32609 MW; 3C98821EC7C60B15 CRC64;
MKAANVLETI GKTPHIRLSR LFPDHEVWVK SERANPGGSI KDRIALAMVE DAEKAGALKP
GGTIIEPTSG NTGIGLAMVA AVKGYKLVLV MPESMSVERR RLMLAYGATF DLTPKEKGMK
GAIERASELA AKTEGAWVPS QFDNEANWKV HVETTAREIL EDFRDTPVDV LITGVGTGGH
LTGCAEELKR EWAGMKAFAV EPDLSPVISG GQPGPHPIQG IGAGFIPGNL HTQAIDGAIQ
VTAEEAKDMA RRCARTEGLL VGISSGATLA AIANKLDDLD PGSRVLGFNY DTGERYLSVP
DFLPEE
//
