ID Q74EL8_GEOSL Unreviewed; 377 AA.
AC Q74EL8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Cystathionine gamma-synthase/beta-lyase {ECO:0000313|EMBL:AAR34271.1};
GN Name=metC-1 {ECO:0000313|EMBL:AAR34271.1};
GN OrderedLocusNames=GSU0944 {ECO:0000313|EMBL:AAR34271.1};
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR34271.1, ECO:0000313|Proteomes:UP000000577};
RN [1] {ECO:0000313|EMBL:AAR34271.1, ECO:0000313|Proteomes:UP000000577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA
RC {ECO:0000313|Proteomes:UP000000577};
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.,
RA Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.,
RA Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M.,
RA Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.,
RA Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R.,
RA Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
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}.
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DR EMBL; AE017180; AAR34271.1; -; Genomic_DNA.
DR RefSeq; NP_951998.1; NC_002939.5.
DR RefSeq; WP_010941612.1; NC_002939.5.
DR AlphaFoldDB; Q74EL8; -.
DR SMR; Q74EL8; -.
DR STRING; 243231.GSU0944; -.
DR EnsemblBacteria; AAR34271; AAR34271; GSU0944.
DR KEGG; gsu:GSU0944; -.
DR PATRIC; fig|243231.5.peg.949; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_7; -.
DR InParanoid; Q74EL8; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 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 Reference proteome {ECO:0000313|Proteomes:UP000000577}.
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 377 AA; 41165 MW; 35A171E0D3348AF6 CRC64;
MNIATQAAQI GLDWDTRTGA VTVPIYQTAT FRHPGLGQST GYDYSRSGNP TRQALEEGIA
RLDGGARGFA YASGMAAIAN LLLLFKSGDH LVVTEDLYGG TCRLFDQILV QYGLSFTYVD
TSDPEAVRDA IRPETRALFV ESLTNPLLKV ADIAALSTLC RERGLLCIVD NTFLTPYLLR
PLDLGADITV YSGTKYLSGH NDTVSGLVVV KEPALAERVY FLQNSVGAVL GPQDAWLTIR
GMKTLSVRLD RQQENAGRIA EWLARHPRVP RVFYPGLPGH PGHELLARQA RGFGAMIAFE
VDDKALVERL LLKTELISFA ESLGGVETLI TFPQVQTHAD IPPEVRERLG INDVLLRLSV
GIEDADDLIA DLSRAFA
//
