ID E1IW16_ECOLX Unreviewed; 434 AA.
AC E1IW16;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:EFO56510.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:EFO56510.1};
GN Name=metB {ECO:0000313|EMBL:EFO56510.1};
GN ORFNames=HMPREF9348_04407 {ECO:0000313|EMBL:EFO56510.1};
OS Escherichia coli MS 145-7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679204 {ECO:0000313|EMBL:EFO56510.1, ECO:0000313|Proteomes:UP000003691};
RN [1] {ECO:0000313|EMBL:EFO56510.1, ECO:0000313|Proteomes:UP000003691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 145-7 {ECO:0000313|EMBL:EFO56510.1,
RC ECO:0000313|Proteomes:UP000003691};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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|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:EFO56510.1}.
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DR EMBL; ADWS01000032; EFO56510.1; -; Genomic_DNA.
DR AlphaFoldDB; E1IW16; -.
DR Proteomes; UP000003691; Unassembled WGS sequence.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); 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; IPR011821; O_succ_thio_ly.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR02080; O_succ_thio_ly; 1.
DR PANTHER; PTHR11808:SF75; 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 Transferase {ECO:0000313|EMBL:EFO56510.1}.
FT MOD_RES 246
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 434 AA; 47167 MW; C74324A1BA80685C CRC64;
MHIILTAIWD LLNLYAKKFR CPDVLTSINT MFTLVPDISP TKPRELHHMT RKQATIAVRS
GLNDDEQYGC VVPPIHLSST YNFTGFNEPR AHDYSRRGNP TRDVVQRALA ELEGGAGAVL
TNTGMSAIHL VTTVFLKPGD LLVAPHDCYG GSYRLFDSLA KRGCYRVLFV DQGDEQALRA
ALAEKPKLVL VESPSNPLLR VVDIAKICHL AREVGAVSVV DNTFLSPALQ NPLALGADLV
LHSCTKYLNG HSDVVAGVVI AKDPDVVTEL AWWANNIGVT GGAFDSYLLL RGLRTLVPRM
ELAQRNAQAI VKYLQTQPLV KKLYHPSLPE NQGHEIAARQ QKGFGAMLSF ELDGDEQTLR
RFLSGLSLFT LAESLGGVES LISHAATMTH AGMAPEARAA AGISETLLRI STGIEDGEDL
IADLENGFRA ANKG
//
