ID G5H5N9_9BACT Unreviewed; 427 AA.
AC G5H5N9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9450_00249 {ECO:0000313|EMBL:EHB93478.1};
OS Alistipes indistinctus YIT 12060.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=742725 {ECO:0000313|EMBL:EHB93478.1, ECO:0000313|Proteomes:UP000006008};
RN [1] {ECO:0000313|EMBL:EHB93478.1, ECO:0000313|Proteomes:UP000006008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12060 {ECO:0000313|EMBL:EHB93478.1,
RC ECO:0000313|Proteomes:UP000006008};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Alistipes indistinctus YIT 12060.";
RL Submitted (AUG-2011) 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:EHB93478.1}.
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DR EMBL; ADLD01000003; EHB93478.1; -; Genomic_DNA.
DR RefSeq; WP_009133055.1; NZ_JH370371.1.
DR AlphaFoldDB; G5H5N9; -.
DR STRING; 742725.HMPREF9450_00249; -.
DR GeneID; 78318097; -.
DR PATRIC; fig|742725.3.peg.282; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_2_10; -.
DR OrthoDB; 9803729at2; -.
DR Proteomes; UP000006008; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006008}.
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 427 AA; 46312 MW; 335240E609B93E78 CRC64;
MNEKLKPATL CVQAGWTPKK GEPRVLPIYQ STTFKYETSD QMARLFDLEE SGYFYTRLQN
PTNDAVAAKI AALEGGVAAM LTSSGQAANF YAVLNLCSAG DHFVSAATVY GGTFNLFAVT
MAKMGIEVTF IDQDASEEEI AAAFRPNTKL LFGETITNPG VEVLDIEKFA RIAHNHGVPL
IVDNTFATPI NCRPFEWGAD IVTHSTTKYM DGHATAVGGA IVDSGNFDWE AHADKFPGLT
QPDPSYHGLT YSTAFGKGAY ITKATVQLMR DLGSIQAPQN AFLLNLGLET LDLRMERHCK
NAQQVAEYLR SNDQVAWVHY PGLQGDKYYE LGQKYLPKGS CGVIAFGLKG GREESIRFMD
ALKLCAIVTH VADARTSVLH PASHTHRQLT DEQLAAAGVA PDLIRLSVGI EDAGDIIADI
AQALAAR
//
