ID E2ZNM7_9FIRM Unreviewed; 424 AA.
AC E2ZNM7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase {ECO:0000313|EMBL:EFQ05271.1};
GN ORFNames=HMPREF9436_03295 {ECO:0000313|EMBL:EFQ05271.1};
OS Faecalibacterium cf. prausnitzii KLE1255.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=748224 {ECO:0000313|EMBL:EFQ05271.1, ECO:0000313|Proteomes:UP000006028};
RN [1] {ECO:0000313|EMBL:EFQ05271.1, ECO:0000313|Proteomes:UP000006028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLE1255 {ECO:0000313|EMBL:EFQ05271.1,
RC ECO:0000313|Proteomes:UP000006028};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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:EFQ05271.1}.
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DR EMBL; AECU01000245; EFQ05271.1; -; Genomic_DNA.
DR RefSeq; WP_005946495.1; NZ_GL538350.1.
DR AlphaFoldDB; E2ZNM7; -.
DR STRING; 748224.HMPREF9436_03295; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_2_9; -.
DR OrthoDB; 9780685at2; -.
DR BioCyc; FCF748224-HMP:GTSS-1549-MONOMER; -.
DR Proteomes; UP000006028; 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 Transferase {ECO:0000313|EMBL:EFQ05271.1}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 424 AA; 45735 MW; 9168E4F469A05545 CRC64;
MNRDTICVQG GYTPGNGEPR QIPIIQSTTF KYATSEDMGK LFDLEADGYF YSRLQNPTCD
LVAKKICELE GGTAAMLTSS GQAANFFALF NLCEAGDHIV ASSTIYGGTF NLISVTMKKM
GIEATFVDPL CTEEELNAAF QPNTKVVFGE TIANPALTVL DIEKFAKAAH AHGVPLIVDN
TFPTPVNCRP FEWGADIVTH STTKYMDGHG AVLGGAIVDG GKFDWMAHAE KFPGLCTPDD
SYHGITYAER FGKEGAFITK ATAQLMRDFG SMQSPMNAYM LNLGLESLHV RMQRHCANGM
AVAEFLESHP KVAYVNYCGL ESSPYHALAE KYLPNGSCGV VSFGLAGGRE AASIFMKNLK
LAAIETHVAD ARTCCLNPAS STHRQMNDEQ LKAAGVPAEL VRMSCGLESS EDLIADIAQA
LDKI
//