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
//