ID   M4RFV2_9BIFI            Unreviewed;       438 AA.
AC   M4RFV2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Ahsa2 {ECO:0000313|EMBL:AGH41054.1};
GN   ORFNames=D805_0787 {ECO:0000313|EMBL:AGH41054.1};
OS   Bifidobacterium thermophilum RBL67.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1254439 {ECO:0000313|EMBL:AGH41054.1, ECO:0000313|Proteomes:UP000011835};
RN   [1] {ECO:0000313|EMBL:AGH41054.1, ECO:0000313|Proteomes:UP000011835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RBL67 {ECO:0000313|EMBL:AGH41054.1,
RC   ECO:0000313|Proteomes:UP000011835};
RX   PubMed=23640377;
RA   Jans C., Lacroix C., Follador R., Stevens M.J.;
RT   "Complete Genome Sequence of the Probiotic Bifidobacterium thermophilum
RT   Strain RBL67.";
RL   Genome Announc. 1:E00191-13(2013).
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; CP004346; AGH41054.1; -; Genomic_DNA.
DR   RefSeq; WP_015450313.1; NC_020546.1.
DR   AlphaFoldDB; M4RFV2; -.
DR   KEGG; btp:D805_0787; -.
DR   PATRIC; fig|1254439.12.peg.783; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_0_11; -.
DR   Proteomes; UP000011835; 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: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}.
FT   MOD_RES         212
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   438 AA;  47565 MW;  2E00F5883D60793E CRC64;
     MAEKNNHYRF ETLQLHVGQE EADPATDSRA VPIYATTSYV FHDFDHAEAR FGLQDPGNIY
     GRLTNTTEGV FEDRIAALEG GTAGLAVASG AAAVEYAVRN ITQTGDHIVA SKHIYGGTFN
     LLRHTLPRDG VNTTFVEPSD PKNFEDAIQE NTKLVYIETF GNPNSDLADI EAIADIAHKH
     NLPLVVDNTF ATPYLFRPLE HGADIVVESA TKFIGGHGTT LGGVIVEGGK FDWAAVPGKF
     PTLTEPDPSY HNLNFYEALG PVAFVTRARA ILLRDTGATL SPFAAFLLLQ GTETLSLRVE
     RHVQNALKVV EYLQTVPEVE SVSHPAVPGR PDHDLYAKYF PNGGGSIFTF DIKGGKDAAR
     VFINNLHLFS LLANVGDAKS LVVHPASTTH SQESPEELED QGIHQGTIRL SIGLENIDDI
     IEDLEGGFKA LRESGLAK
//