ID F2CDZ9_STRSA Unreviewed; 426 AA.
AC F2CDZ9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:EGF19204.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:EGF19204.1};
GN Name=metY {ECO:0000313|EMBL:EGF19204.1};
GN ORFNames=HMPREF9391_1015 {ECO:0000313|EMBL:EGF19204.1};
OS Streptococcus sanguinis SK408.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888818 {ECO:0000313|EMBL:EGF19204.1, ECO:0000313|Proteomes:UP000004826};
RN [1] {ECO:0000313|EMBL:EGF19204.1, ECO:0000313|Proteomes:UP000004826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK408 {ECO:0000313|EMBL:EGF19204.1,
RC ECO:0000313|Proteomes:UP000004826};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) 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}.
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:EGF19204.1}.
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DR EMBL; AFBE01000008; EGF19204.1; -; Genomic_DNA.
DR RefSeq; WP_002917444.1; NZ_GL878559.1.
DR AlphaFoldDB; F2CDZ9; -.
DR PATRIC; fig|888818.3.peg.982; -.
DR HOGENOM; CLU_018986_4_0_9; -.
DR Proteomes; UP000004826; Unassembled WGS sequence.
DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; 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; 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.
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:EGF19204.1}.
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 426 AA; 46221 MW; E3D4340A4EB0AC89 CRC64;
MTREFKFETL QLHAGQTVDP TTKSRALPIY QTTSYVFDDT QEGEDLFALR KPGNIYTRIT
NPTLSAFEER IAALEGGVGA LATASGMAAV TYTILALAHA GDHVVAASTI YGGTFNLLKE
TLPRYGITTT FVDIENLAEV EAAIQDNTKL VLIESLGNPL INIPDFDALA ELVHAHRIPL
ISDNTFATPY LINVFSRGVD IAVHSATKFI GGHGTSIGGV IVDSGRFDWE ASGKFPQFVD
PDPSYHDISY TRDVGAAAFV TAVRTQLLRD TGAAMSPFNA FLFLQGLETL SLRVERHVSN
AEKIVEFLAG HPKVEQVNYP KLADSPYHTL AEKYFPKGVG SIFTFNVKGG EKEARKVIDS
LEIFSDLANV ADAKSLVVHP ATTTHGQMSP ETQLAAGIKP NQIRLSIGLE NVDDLIEDLK
IALESI
//