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Database: UniProt
Entry: G4FJM4_9SYNE
LinkDB: G4FJM4_9SYNE
Original site: G4FJM4_9SYNE 
ID   G4FJM4_9SYNE            Unreviewed;       440 AA.
AC   G4FJM4;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=O-acetylhomoserine/O-acetylserine sulfhydrylase {ECO:0000313|EMBL:EHA63218.1};
DE            EC=2.5.1.47 {ECO:0000313|EMBL:EHA63218.1};
GN   ORFNames=Syn8016DRAFT_0259 {ECO:0000313|EMBL:EHA63218.1};
OS   Synechococcus sp. WH 8016.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=166318 {ECO:0000313|EMBL:EHA63218.1, ECO:0000313|Proteomes:UP000002752};
RN   [1] {ECO:0000313|EMBL:EHA63218.1, ECO:0000313|Proteomes:UP000002752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8016 {ECO:0000313|Proteomes:UP000002752};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Palenik B., Woyke T.J.;
RT   "The draft genome of Synechococcus sp. WH 8016.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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:EHA63218.1}.
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DR   EMBL; AGIK01000001; EHA63218.1; -; Genomic_DNA.
DR   RefSeq; WP_006852398.1; NZ_AGIK01000001.1.
DR   AlphaFoldDB; G4FJM4; -.
DR   STRING; 166318.Syn8016DRAFT_0259; -.
DR   PATRIC; fig|166318.3.peg.287; -.
DR   eggNOG; COG2873; Bacteria.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000002752; 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:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR   PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR   PANTHER; PTHR43797:SF2; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Transferase {ECO:0000313|EMBL:EHA63218.1}.
FT   MOD_RES         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   440 AA;  47287 MW;  C46326B9BF3E8A86 CRC64;
     MTSQRFETLQ LHAGQVPDPT TNSRAVPIYQ TSSYVFNNAE HGANLFGLKE FGNIYTRLMN
     PTTDVFEKRV AALEGGVAAV ATASGQSAQF LAITNCMQAG DNFVSTSFLY GGTYNQFKVQ
     FPRLGIQVKF ADGDDVASFA AQIDDNTKAI YVEAMGNPRF NIPDFAGLSA LAKERGIPLI
     VDNTLGAAGA LIRPIEHGAD VVVESATKWI GGHGTSLGGV IVDAGTFNWG NGKFPLMSQP
     SAAYHGLVHW DAFGFGSDIC KMLGLPDERN IAFALRARVE CLRDWGPAIS PFNSFLLLQG
     LETLSLRVER HAQNAMALAT WLQEHSSVAH VSYPGLPSDP YHASAKRYLT NRGMGCMLMF
     SLKGGCDDAV RFIDSLKLAS HLANVGDSKT LVIHPASTTH QQLSADEQAS AGVTPTMVRV
     SVGLEHIDDI KADFEQALAS
//
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