ID A0A081PD32_9SPHI Unreviewed; 434 AA.
AC A0A081PD32;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:KEQ28605.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:KEQ28605.1};
GN ORFNames=N180_12450 {ECO:0000313|EMBL:KEQ28605.1};
OS Pedobacter antarcticus 4BY.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1358423 {ECO:0000313|EMBL:KEQ28605.1, ECO:0000313|Proteomes:UP000028007};
RN [1] {ECO:0000313|EMBL:KEQ28605.1, ECO:0000313|Proteomes:UP000028007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4BY {ECO:0000313|EMBL:KEQ28605.1,
RC ECO:0000313|Proteomes:UP000028007};
RA Shivaji S., Ray M.K., Rao N.S., Saiserr L., Jagannadham M.V., Kumar G.S.,
RA Reddy G., Bhargava P.M.;
RT "Sphingobacterium antarcticus sp. nov. a Psychrotrophic Bacterium from the
RT Soils of Schirmacher Oasis, Antarctica.";
RL Int. J. Syst. Bacteriol. 42:102-106(1992).
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:KEQ28605.1}.
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DR EMBL; JNFF01000111; KEQ28605.1; -; Genomic_DNA.
DR RefSeq; WP_037443944.1; NZ_JNFF01000111.1.
DR AlphaFoldDB; A0A081PD32; -.
DR eggNOG; COG2873; Bacteria.
DR OrthoDB; 9773476at2; -.
DR Proteomes; UP000028007; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000028007};
KW Transferase {ECO:0000313|EMBL:KEQ28605.1}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 434 AA; 47487 MW; 40570B508D55C8F8 CRC64;
MSANYKFETL QIHAGQEIDP TTGSRAVPIY QTTSYGFKSA EHGANLFALK EFGNIYTRLM
NPTTDVFEKR IAALEGGVAA LAVSSGQAAQ FIALSNFLQA GDNFVSSPHL YGGTYNQFKV
AFKRLGIDAK FAATDQVEDF EAQIDNNTKG IYLESIGNPS FSIPDFEKLA LLAQKYDIPL
VVDNTFGAAG YLFKPLEHGA HIVVQSATKW IGGHGTSVGG VIVDGGNYNW GNGKFEQFSK
PSPGYHGLVF SDVFGVNSEL GNIQFIIRAR VEGLRDFGPS QSPFNSFLLI QGLETLSLRV
QRHVDNALAL ANWLENHEAV KKVYYPGLES SPYHLNAKKY LKNGFGAVLS FELEGDKDQT
INFVNSLELV SHLANVGDAK TLIIQPSATT HQQLNEEEQL AAGITPQLLR VSVGIEHIDD
IKADFEQAFE KIKL
//
