ID A0A0A8X532_9BACI Unreviewed; 462 AA.
AC A0A0A8X532;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=O-acetylhomoserine sulfhydrylase /O-succinylhomoserine sulfhydrylase {ECO:0000313|EMBL:GAM14349.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:GAM14349.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:GAM14349.1};
GN ORFNames=SAMD00020551_2498 {ECO:0000313|EMBL:GAM14349.1};
OS Mesobacillus selenatarsenatis SF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1321606 {ECO:0000313|EMBL:GAM14349.1, ECO:0000313|Proteomes:UP000031014};
RN [1] {ECO:0000313|EMBL:GAM14349.1, ECO:0000313|Proteomes:UP000031014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-1 {ECO:0000313|EMBL:GAM14349.1,
RC ECO:0000313|Proteomes:UP000031014};
RA Kuroda M., Sei K., Yamashita M., Ike M.;
RT "Whole genome shotgun sequence of Bacillus selenatarsenatis SF-1.";
RL Submitted (JUN-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:GAM14349.1}.
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DR EMBL; BASE01000054; GAM14349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A8X532; -.
DR STRING; 1321606.SAMD00020551_2498; -.
DR Proteomes; UP000031014; Unassembled WGS sequence.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000031014};
KW Transferase {ECO:0000313|EMBL:GAM14349.1}.
FT COILED 428..455
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 235
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 462 AA; 49776 MW; C1A1DD905A9141E3 CRC64;
MTLFLGRGFF VSVFLKKFLI GEMEMANEQK NYRIETLGVH GGQSPDPVTG ARAVPIYSSN
AFQFENTEHA ADLFALKEAG YIYSRIHNPT VTALEEKVAL LEGGIGALAL SSGMSAITMA
ILNIAHAGDE IVAASNLYGG TYNLFAVTLP KYGIKVHLVD PADPENFRKA ITPKTKAVYA
ETIGNPSLRV LDIEAVAEVA HEADLPLIID NTFATPYLCR PIEHGADIVV HSATKWLLGN
GTVMGGIIVD GGKFDWKSPK FPGFNEPDSS YHDLVYSEAI GAAAFIVKAR VQLLRDLGPA
ISPQSAFQFN LGIETLHVRM KEHVANTRKI VDYLESHPAV TWVSYPGHES HPDKELADRY
LPKGAGAVVI FGIEGGRESG AKLINSLELW SHVANVGDAK SLIIHPASTT HQQLDSEGLK
AAGVPEDLIR LSVGIENAED IIEDLEQAIE KATGVPGIPA RA
//
