ID M7MWR0_9MICC Unreviewed; 445 AA.
AC M7MWR0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:EMQ99506.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:EMQ99506.1};
GN ORFNames=ADIAG_01502 {ECO:0000313|EMBL:EMQ99506.1};
OS Paeniglutamicibacter gangotriensis Lz1y.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Paeniglutamicibacter.
OX NCBI_TaxID=1276920 {ECO:0000313|EMBL:EMQ99506.1, ECO:0000313|Proteomes:UP000012015};
RN [1] {ECO:0000313|EMBL:EMQ99506.1, ECO:0000313|Proteomes:UP000012015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lz1y {ECO:0000313|EMBL:EMQ99506.1,
RC ECO:0000313|Proteomes:UP000012015};
RX PubMed=23766407;
RA Shivaji S., Ara S., Bandi S., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Arthrobacter gangotriensis Strain Lz1yT, Isolated
RT from a Penguin Rookery Soil Sample Collected in Antarctica, near the Indian
RT Station Dakshin Gangotri.";
RL Genome Announc. 1:e00347-e00313(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:EMQ99506.1}.
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DR EMBL; AOCK01000003; EMQ99506.1; -; Genomic_DNA.
DR RefSeq; WP_007270694.1; NZ_AOCK01000003.1.
DR AlphaFoldDB; M7MWR0; -.
DR STRING; 1276920.ADIAG_01502; -.
DR PATRIC; fig|1276920.7.peg.1500; -.
DR eggNOG; COG2873; Bacteria.
DR Proteomes; UP000012015; 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 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 Lyase {ECO:0000313|EMBL:EMQ99506.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000012015};
KW Transferase {ECO:0000313|EMBL:EMQ99506.1}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 445 AA; 46327 MW; 3699B8A08B5D7700 CRC64;
MASSSWQNAT TEIHAGYSPT GEHRPMTVPI YNTAAYQFPD YATAARLFSL KEPGFTYSRT
GNPTVAVLEE RAAALEGGIG AIATATGQAA VALSLLALLQ GPNHLVASNK LYGGTVDLLT
DTFADFGITV TFVDPEDPAN WAAAITEKTR GFLLESVSNP LATLVDLRVI TDLAHAAGIP
VVVDNTLATP AACRPIEFGA DIVVHSATKA LSGHGSVLGG LIIDAGTFDF TDAARWPQIA
GPKARYGGDL LLGRYGAKAY LMLARSKFLH DLGPTLSAAS ASSILTGIET LSLRVAKAQA
NVLELVKALG GHPAVARVHH PSVPTHQDHE LAKEYFPNGT GCVFSFDLVD AAAVPQLVDS
LKLFALAANI GDARSLIVHP AAMTHCRLND EQLAAAGIAP GTLRLSVGLE DAGDLVDDLI
TGLDGLGRNN TSETVANAPR TSINA
//
