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Database: UniProt
Entry: B5JDA9_9BACT
LinkDB: B5JDA9_9BACT
Original site: B5JDA9_9BACT 
ID   B5JDA9_9BACT            Unreviewed;       427 AA.
AC   B5JDA9;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase subfamily {ECO:0000313|EMBL:EDY83813.1};
GN   ORFNames=VDG1235_3440 {ECO:0000313|EMBL:EDY83813.1};
OS   Verrucomicrobiae bacterium DG1235.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae.
OX   NCBI_TaxID=382464 {ECO:0000313|EMBL:EDY83813.1, ECO:0000313|Proteomes:UP000003839};
RN   [1] {ECO:0000313|EMBL:EDY83813.1, ECO:0000313|Proteomes:UP000003839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG1235 {ECO:0000313|EMBL:EDY83813.1,
RC   ECO:0000313|Proteomes:UP000003839};
RA   Hart M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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}.
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DR   EMBL; DS990592; EDY83813.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5JDA9; -.
DR   STRING; 382464.VDG1235_3440; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_0_0; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000003839; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000003839};
KW   Transferase {ECO:0000313|EMBL:EDY83813.1}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         204
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   427 AA;  45990 MW;  0DA339DE58D517C0 CRC64;
     MNIETKCLHA GQEPDPTTKS RGVPVYRTTS YVFDNTEHAA NLFALKELGN IYTRIMNPTQ
     DVLEKRVAAM EGGAAALALA SGTSAIFYTI INLAQHGDNI VSANNLYGGT YTQFSNILPA
     FGINVKFVDP TDPEAVANSI DEHTRAVFCE SVGNPGLDVT DIQALADVAH ARGLPLVVDA
     TFSTPYLTRP IEHGADIVVH SLTKWLGGHG AGIGGIVVDS GAFNWANGNF PLYDQPDDSY
     HGLRWGHDLP EPLAPLAFIL RMRTVPLRNL GACISPDNSW FILQGIETLH LRMERHCENA
     LAVAKHLQSL DTVDWVKYPG LEDNPNYEKA QKYLDGKGGS MVVFGIKGGA PAGSRFIDAL
     ELLSHLANVG DAKSLAIHPA TTTHSQLSQE EQRLGGISPE LIRLSVGIEN VSDIIADIDQ
     ALAKAVV
//
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