ID R9N2F1_9FIRM Unreviewed; 428 AA.
AC R9N2F1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase {ECO:0000313|EMBL:EOS77146.1};
GN ORFNames=C819_01172 {ECO:0000313|EMBL:EOS77146.1};
OS Lachnospiraceae bacterium 10-1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235800 {ECO:0000313|EMBL:EOS77146.1, ECO:0000313|Proteomes:UP000014134};
RN [1] {ECO:0000313|EMBL:EOS77146.1, ECO:0000313|Proteomes:UP000014134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-1 {ECO:0000313|EMBL:EOS77146.1,
RC ECO:0000313|Proteomes:UP000014134};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 10-01.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EOS77146.1}.
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DR EMBL; ASTF01000010; EOS77146.1; -; Genomic_DNA.
DR AlphaFoldDB; R9N2F1; -.
DR STRING; 1235800.C819_01172; -.
DR PATRIC; fig|1235800.3.peg.1257; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_2_9; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000014134; 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 NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR PANTHER; PTHR43797:SF3; O-ACETYLHOMOSERINE SULFHYDRYLASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000014134};
KW Transferase {ECO:0000313|EMBL:EOS77146.1}.
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 428 AA; 46407 MW; D8CD1E1ABAB5657A CRC64;
MSDYKMNTKC VQAGYTPENG EPRQIPIFQS TTFKYATSED MGKLFDLEAS GYFYSRLQNP
TNDHVAAKIA ELEGGTAAML TSSGQAANFF ALFNICECGS HIVSSSSIYG GTFNLISVTM
AKMGVEVTFV SPDCTKEELD EAFQENTKAV FGESIANPAL TVLDIEKFAK AAHKHGVPLI
VDNTFPTPVN CRPIEWGADI VTHSTTKYMD GHGAAVGGAI IDSGKFDWMA YADKFPGLCT
PDESYHGITY AEKFGKEGAF ITKCTSQLMR DLGCVQSPQN AFILNLGLES LHVRMPRHVE
NGQAVAEFLS GQPQVSYVNY PGLKGNKYYE TAKKYMPNGG CGVVSFELKG GREAAETFMK
HLKLAAIETH VADARTCCLN PATTTHRQMS EEQLKEAGVP AGLIRISCGL EDKEDLIADL
AQALAAIN
//