ID A0A0K1RE80_9CORY Unreviewed; 386 AA.
AC A0A0K1RE80;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:AKV59740.1};
GN ORFNames=AK829_00310 {ECO:0000313|EMBL:AKV59740.1};
OS Corynebacterium riegelii.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=156976 {ECO:0000313|EMBL:AKV59740.1, ECO:0000313|Proteomes:UP000060016};
RN [1] {ECO:0000313|EMBL:AKV59740.1, ECO:0000313|Proteomes:UP000060016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PUDD_83A45 {ECO:0000313|EMBL:AKV59740.1,
RC ECO:0000313|Proteomes:UP000060016};
RA Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL Submitted (AUG-2015) 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}.
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DR EMBL; CP012342; AKV59740.1; -; Genomic_DNA.
DR RefSeq; WP_052206272.1; NZ_CP068159.1.
DR AlphaFoldDB; A0A0K1RE80; -.
DR STRING; 156976.AK829_00310; -.
DR PATRIC; fig|156976.3.peg.56; -.
DR Proteomes; UP000060016; Chromosome.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
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: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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000060016}.
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 386 AA; 41438 MW; 7293960C0B99D775 CRC64;
MSTNTSNPGP STAAIHAGYE PDSLYGPINT PIYASTTFAQ NGLAELRGGY EYTRVGNPTI
TALEKSVAAL EGADFAVAFA SGMATVDVVL RTLLKPGDHI VVSNDAYGGT YRLIQQVFSL
WGVENTVVDM TNAEEVGAAV QDNTKVIWVE TPTNPLLSIV DIEAVAKVKG GAALVVDNTF
ASPYLQRPFE FGADVVLHST TKYIGGHSDV IGGVVCGKDD LIEGFEEQLR FFFGWVGAIP
SPFDTYLTGR GLKTLPVRME RHCDNAEAVA KYLEGRKEVA RVCYPGLESH PGHEVAKKQM
RRFGGMVSVL FQTEEQAKKF CLSTQLFCLA ESLGGVESLL EHPATMTHVS VAGSALEVPG
ELVRISVGIE DEADLIADLE QAFAQL
//
