ID A0A261G4M2_9BIFI Unreviewed; 429 AA.
AC A0A261G4M2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:OZG66370.1};
GN ORFNames=BHAP_0232 {ECO:0000313|EMBL:OZG66370.1};
OS Bifidobacterium hapali.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1630172 {ECO:0000313|EMBL:OZG66370.1, ECO:0000313|Proteomes:UP000216074};
RN [1] {ECO:0000313|EMBL:OZG66370.1, ECO:0000313|Proteomes:UP000216074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100202 {ECO:0000313|EMBL:OZG66370.1,
RC ECO:0000313|Proteomes:UP000216074};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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:OZG66370.1}.
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DR EMBL; MWWY01000005; OZG66370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261G4M2; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000216074; Unassembled WGS sequence.
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 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Transferase {ECO:0000313|EMBL:OZG66370.1}.
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 429 AA; 45735 MW; 7C64A63D111092A6 CRC64;
MTDLTTKAIH AGYDRAANAR AANVPIYASA AFDLENAERG RALAAGELDG FEYSRVANPT
VDVLERRLAA LEGGIGAVAV SSGMAAVSYA LMCVGESGGR IIASKNLYGA SVDALVDFLP
EFGIHADFVT DINDLAEVES KIGPDTRAIY TETVANPSTE IADLEPLADL AHRHGIALIV
DNTVPTPYLL RPIEFGADIV VHSTTKGITG HGNAIGGAII DAGHFDWANG RFPQFTRPQQ
VIADADGKPR TFAGAFGSEA FIRRIRIKYL RTFGAVQSPF NAYLTLVGLE TLPERVSRQV
ATATTVARHL TRTPHVLTVN YSGLGDTPQY ALAAKYLPHG VGQILSFTVD GDRANVQRIL
DGTKLFSYVP NIGDARSLIV DPANITHREV PDDVRRAAGV TSNLIRLSIG LESADDLIAD
LDQAIANAY
//
