ID Q2IEA5_ANADE Unreviewed; 426 AA.
AC Q2IEA5;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:ABC82912.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:ABC82912.1};
GN OrderedLocusNames=Adeh_3143 {ECO:0000313|EMBL:ABC82912.1};
OS Anaeromyxobacter dehalogenans (strain 2CP-C).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC82912.1, ECO:0000313|Proteomes:UP000001935};
RN [1] {ECO:0000313|Proteomes:UP000001935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA Zhulin I.B., Loeffler F.E., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL Submitted (JAN-2006) 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}.
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DR EMBL; CP000251; ABC82912.1; -; Genomic_DNA.
DR RefSeq; WP_011422194.1; NC_007760.1.
DR AlphaFoldDB; Q2IEA5; -.
DR STRING; 290397.Adeh_3143; -.
DR KEGG; ade:Adeh_3143; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_7; -.
DR OrthoDB; 9790858at2; -.
DR Proteomes; UP000001935; Chromosome.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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 Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW Transferase {ECO:0000313|EMBL:ABC82912.1}.
FT MOD_RES 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 426 AA; 45548 MW; 9E05A7E7C2FF6164 CRC64;
MTEDVHLDSN VPGNPAYHFT IVPPGTPARA GWTERAPLVP GAGLATQCVH AGVQPDPAYG
AVMPPIYQSS TFAFRDVCTN AGYDYTRSGN PTRAALEEAI ATLEGGAGAT CTTTGMAAVL
VALNLLPHGS HLLCTVDCYG GTFRTLEHAR QAYGLEVTYL DLADLGAVER ALRPNTGMVW
IETPSNPLLR LTDIRAVTEL AHRRGALVVV DNTFLSPALQ RPFEHGADLV VHSTTKYLNG
HSDVVGGAVV APRDRTALLQ RIQSMNNLLG TSQGPHDAFL VLRGLKTLAL RVKAHEAGAR
RVAAFLAGHP EVARVHYPGL ASHPQHALAR AQQRGFGAML SFELRDGRPD RVDHVLRTLR
WFTLAESLGG VESLVAHPAS MTHASMTPEA RQRAGITDSV IRLSIGIEEP EDLLGDLDRA
LASLPA
//
