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Database: UniProt
Entry: H0TLY6_9BRAD
LinkDB: H0TLY6_9BRAD
Original site: H0TLY6_9BRAD 
ID   H0TLY6_9BRAD            Unreviewed;       434 AA.
AC   H0TLY6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase (O-acetylhomoserine (Thiol)-lyase or OAH sulfhydrylase) {ECO:0000313|EMBL:CCE07474.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:CCE07474.1};
GN   Name=metY {ECO:0000313|EMBL:CCE07474.1};
GN   ORFNames=BRAS3843_2130017 {ECO:0000313|EMBL:CCE07474.1};
OS   Bradyrhizobium sp. STM 3843.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE07474.1, ECO:0000313|Proteomes:UP000002686};
RN   [1] {ECO:0000313|Proteomes:UP000002686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX   PubMed=24704842; DOI=10.3390/genes3010035;
RA   Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA   Smith A.A., Giraud E., Medigue C., Moulin L.;
RT   "Comparative genomics of aeschynomene symbionts: insights into the
RT   ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL   Genes (Basel) 3:35-61(2011).
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:CCE07474.1}.
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DR   EMBL; CAFK01000128; CCE07474.1; -; Genomic_DNA.
DR   RefSeq; WP_008969991.1; NZ_CAFK01000128.1.
DR   AlphaFoldDB; H0TLY6; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000002686; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   Lyase {ECO:0000313|EMBL:CCE07474.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002686};
KW   Transferase {ECO:0000313|EMBL:CCE07474.1}.
FT   MOD_RES         204
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   434 AA;  46958 MW;  63FD61E1A917B8EE CRC64;
     MRNETIAIHA GYEPDPTTKA VAVPIYQTAA YAFDSADHGA ALFNLEAEGY RYSRISNPTT
     AVLEKRVSEL EGGVGALAVG TGQAALHFAF VNLADHGGNI VSVPQLYGTT HTLLGHILPR
     QGIIGRFAES DQPDAIERLI DENTRAVFAE TIGNPAGNVC DIEALAKVAH RNGVPLLVDN
     TVATPILLKP FDYGADIAVH SLTKFLGGHG TTLGGALVDS GNFPWKQHAD RFPAFSQPDT
     SYHGLVYTDH FGKSAFIQRA RSVYQRTMGA VLSPFNAFLL LQGIETVALR MERHVENARK
     VAEFLRDDPR VAWVNYAGFS DSPYYPLVQK YLDGHASSLF TFGIKGGLDA GKAFYDSLKL
     ITRLVNIGDA KSLACHPAST THRQMSADEQ RKAGVLPETI RLSIGIEHIS DIIEDLDQAL
     AQAVARQPRL AAAE
//
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