ID U6SMU0_9BACI Unreviewed; 430 AA.
AC U6SMU0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:ERN52240.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:ERN52240.1};
GN ORFNames=A33I_17175 {ECO:0000313|EMBL:ERN52240.1};
OS Alkalihalophilus marmarensis DSM 21297.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX NCBI_TaxID=1188261 {ECO:0000313|EMBL:ERN52240.1, ECO:0000313|Proteomes:UP000017170};
RN [1] {ECO:0000313|EMBL:ERN52240.1, ECO:0000313|Proteomes:UP000017170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21297 {ECO:0000313|EMBL:ERN52240.1,
RC ECO:0000313|Proteomes:UP000017170};
RX PubMed=24285666;
RA Wernick D.G., Choi K.Y., Tat C.A., Lafontaine Rivera J.G., Liao J.C.;
RT "Genome Sequence of the Extreme Obligate Alkaliphile Bacillus marmarensis
RT Strain DSM 21297.";
RL Genome Announc. 1:e00967-e00913(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}.
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:ERN52240.1}.
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DR EMBL; ATAE01000038; ERN52240.1; -; Genomic_DNA.
DR RefSeq; WP_022629020.1; NZ_ATAE01000038.1.
DR AlphaFoldDB; U6SMU0; -.
DR PATRIC; fig|1188261.3.peg.2935; -.
DR Proteomes; UP000017170; 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:ERN52240.1}.
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 430 AA; 46223 MW; 6F966EABD4C95B40 CRC64;
MSEENHFRPE TLAIHAGQEI DPTTFSRAVP LYQTTSYGFK DTDHAANLFS LSEFGNIYTR
LMNPTTDVFE KRVAALEGGA AALATASGQA AITYSILNIA EAGDEIVSAA SLYGGTYNLF
STTLPKLGIK VHFVDPTDPA NFKAAITDKT KAIYAETVGN PKGDVLDIEA VAHIAHEHNL
PLIVDNTFPS PYLLQPIKHG ADIVVHSATK FIGGHGTSIG GVIVDSGKFD WTKTDKYPGL
TTPDPSYNGV VYTEAVGPIA YIIKARVQLL RDLGASIAPF NSFLLLQGLE TLHLRMKQHS
ENALETARFL EAHQSVDWVS YSGLESHSSY DLAQKYLPKG QGAILTFGLK GGVEAGKKLI
HSVDLFSHLA NVGDSKSLII HPASTTHQQL TEEEQLAAGV TPGMIRLSIG TEAIEDILGD
LGQAIEKSQQ
//