ID   Q6NIY6_CORDI            Unreviewed;       438 AA.
AC   Q6NIY6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=Methionine biosynthesis-related protein {ECO:0000313|EMBL:CAE49147.1};
GN   OrderedLocusNames=DIP0630 {ECO:0000313|EMBL:CAE49147.1};
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=257309 {ECO:0000313|EMBL:CAE49147.1, ECO:0000313|Proteomes:UP000002198};
RN   [1] {ECO:0000313|EMBL:CAE49147.1, ECO:0000313|Proteomes:UP000002198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis
RC   {ECO:0000313|Proteomes:UP000002198};
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.,
RA   Bentley S.D., Besra G.S., Churcher C., James K.D., De Zoysa A.,
RA   Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S.,
RA   Jagels K., Moule S., Quail M.A., Rabbinowitsch E., Rutherford K.,
RA   Thomson N.R., Unwin L., Whitehead S., Barrell B.G.Parkhill.J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(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; BX248355; CAE49147.1; -; Genomic_DNA.
DR   RefSeq; WP_010934433.1; NC_002935.2.
DR   AlphaFoldDB; Q6NIY6; -.
DR   STRING; 257309.DIP0630; -.
DR   KEGG; cdi:DIP0630; -.
DR   HOGENOM; CLU_018986_4_0_11; -.
DR   Proteomes; UP000002198; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; 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; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR   PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR   PANTHER; PTHR43797:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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:UP000002198}.
FT   MOD_RES         217
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   438 AA;  46575 MW;  A20ADC36E74D43D3 CRC64;
     MPTKYDNSNA NKWGFETRSI HAGQSVDSDT SARNLPIYLT SSYVFNDAEH AANRFNLSDA
     GPVYSRLTNP TVAAVEERLA NLEGGVHAVL FASGMAAETA AILNIARAGS HIVSSPRIYG
     GTETLFAVTL ARLGIETTFV ENPDDPASWE AAVQDNTVAL YGETFANPQA DVLDIPAIAE
     VAHKHQVPLI VDNTLATAAL VRPLELGADV VVASLTKFYT GNGSGLGGVL IDGGNFDWTV
     TRNGEPIFPD FVTPDPAYHG LKYSDLGAPA FGLKARVGLL RDTGAAPSPL NAWITAQGLD
     TLSLRVQRHN ENALAVAQFL ANHEKVAKVN YAGLPDSPWY PVKEKLGFDY TGSVLSFDVK
     GGKNEAWRFI DALKLHSNLA NVGDVRSLVV HPATTTHSQS EESALLAAGI NQATIRLSVG
     IESIDDIIAD LTAGFDAI
//