ID X5DHZ7_9CORY Unreviewed; 421 AA.
AC X5DHZ7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:AHW62673.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:AHW62673.1};
GN Name=metB {ECO:0000313|EMBL:AHW62673.1};
GN ORFNames=CGLY_01125 {ECO:0000313|EMBL:AHW62673.1};
OS Corynebacterium glyciniphilum AJ 3170.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW62673.1, ECO:0000313|Proteomes:UP000023703};
RN [1] {ECO:0000313|EMBL:AHW62673.1, ECO:0000313|Proteomes:UP000023703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW62673.1};
RX PubMed=25323597; DOI=10.1099/ijs.0.065102-0;
RA Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J.,
RA Ruckert C.;
RT "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp.
RT nov., nom. rev., isolated from putrefied banana.";
RL Int. J. Syst. Evol. Microbiol. 65:177-182(2015).
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; CP006842; AHW62673.1; -; Genomic_DNA.
DR RefSeq; WP_038545367.1; NZ_CP006842.1.
DR AlphaFoldDB; X5DHZ7; -.
DR STRING; 1404245.CGLY_01125; -.
DR KEGG; cgy:CGLY_01125; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_11; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000023703; Chromosome.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
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: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:UP000023703};
KW Transferase {ECO:0000313|EMBL:AHW62673.1}.
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 421 AA; 44467 MW; 4377F8B22E81313D CRC64;
MSSDDQSGQP NEHETRADAG TAARRAAALQ ARQRLTDAAG RPFGFDTNAI HSGYEPDGQT
GAINTPIYAS TTYAQDGVAQ LRGGFEYSRC GNPTVTALEE TVAALEGAKF GRAFASGMAA
TDTVLRALLH PGAHVILGND AYGGTFRLLD TTYRDWGVEV SVVDTADTRQ VADALRPDTK
LVWLETPTNP LLGITDIAAT ADALKDHPAK LIVDNTFASP YLQRPLALGA DVVMHSTTKY
LGGHSDVVGG VIVTDDEDLD GELLFLQGGV GAVPSPFDAY LTYRGIKTLG LRMDRHCANA
QAVAEFLDGR PEIAQVLYPG LPGHTGHDIA ARQMDGFGAM VSVRFAGGEV PALQFCENTR
LICLAESLGG VESLLEHPAK MTHQSAAGSA LEVPDDLVRI SIGIENVDDL LADLAQALDA
L
//
