ID   E8WLK6_GEOS8            Unreviewed;       417 AA.
AC   E8WLK6;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Cysteine synthase {ECO:0000313|EMBL:ADW13686.1};
DE            EC=2.5.1.47 {ECO:0000313|EMBL:ADW13686.1};
GN   OrderedLocusNames=GM18_2227 {ECO:0000313|EMBL:ADW13686.1};
OS   Geobacter sp. (strain M18).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW13686.1, ECO:0000313|Proteomes:UP000001442};
RN   [1] {ECO:0000313|EMBL:ADW13686.1, ECO:0000313|Proteomes:UP000001442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M18 {ECO:0000313|EMBL:ADW13686.1,
RC   ECO:0000313|Proteomes:UP000001442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Holmes D.,
RA   Aklujkar M., Lovley D., Woyke T.;
RT   "Complete sequence of Geobacter sp. M18.";
RL   Submitted (JAN-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   ---------------------------------------------------------------------------
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; CP002479; ADW13686.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8WLK6; -.
DR   STRING; 443143.GM18_2227; -.
DR   KEGG; geb:GM18_2227; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_0_7; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000001442; Chromosome.
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   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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Transferase {ECO:0000313|EMBL:ADW13686.1}.
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   417 AA;  45219 MW;  6170ED4155AB77CD CRC64;
     MGEGDSRLRF DTKLIHGGTS SGPSGATKPP IVQASAFAYN TAEELEDIFK GRAIGQVYTR
     IGNPTLESLE KRLAVIEDGI AAVVTSSGMS AITTAVMAVV RSGDEILSSS SLFGGTYSLF
     HDTLANYGIK TRFFDPTDLQ ALEDGVNDST RLIFVETIGN PKMDVPDIEA FSALAKKHGI
     PLMVDATVST PYLARMRDLG ADIIIHSTSK YINGTANSIG GAIIDAGSFT WQSDKFPHFE
     QFFRKYRNFA FTARVRKLIH KDFGACAAPF NSFLSGEGLE TLALRMERHC SNALRLAQFL
     YSHEKVAWVN YPGLPDSPFH EVAKRQFDGR FGGLLTFGLA DKAAAFRLIN GLKLAKNLAN
     IGDTKSLVIH PASTICADYT PEVNALMGVS EELVRVSVGV EDPMDILEDF AAALEQV
//