ID A0A0N0Z8S0_9GAMM Unreviewed; 424 AA.
AC A0A0N0Z8S0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=O-acetylhomoserine sulfhydrylase/O-succinylhomoserine sulfhydrylase {ECO:0000313|EMBL:KPD03627.1};
DE EC=2.5.-.- {ECO:0000313|EMBL:KPD03627.1};
DE EC=2.5.1.- {ECO:0000313|EMBL:KPD03627.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:KPD03627.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:KPD03627.1};
GN ORFNames=M992_0917 {ECO:0000313|EMBL:KPD03627.1};
OS Moellerella wisconsensis ATCC 35017.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Moellerella.
OX NCBI_TaxID=1354267 {ECO:0000313|EMBL:KPD03627.1, ECO:0000313|Proteomes:UP000053226};
RN [1] {ECO:0000313|EMBL:KPD03627.1, ECO:0000313|Proteomes:UP000053226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35017 {ECO:0000313|EMBL:KPD03627.1,
RC ECO:0000313|Proteomes:UP000053226};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (JUL-2015) 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:KPD03627.1}.
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DR EMBL; LGAA01000009; KPD03627.1; -; Genomic_DNA.
DR RefSeq; WP_053907509.1; NZ_LGAA01000009.1.
DR AlphaFoldDB; A0A0N0Z8S0; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000053226; 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.
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:UP000053226};
KW Transferase {ECO:0000313|EMBL:KPD03627.1}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 424 AA; 45520 MW; F5547167EAAD65BA CRC64;
MKLETLSIHA GYSPDPTTKA VAVPIYQTTS YAFDDTQHGA DLFDLKVAGN IYSRIMNPTN
DVLEKRVAAL EGGIAGLAVA SGMAAITYAI QTVAQAGDNI VSVAKLYGGT YNLLAHTLPR
FGIETRFAEH DDIAALEALI DDKTKAVFCE SITNPAGFIV DIQALAEAAH RHGVPLIVDN
TVATPCLCRP FEFGADIVVH SLTKYIGGHG TSIGGMVVDS GKFPWAQHKQ RFAILNEPDI
SYHGVSYTEH FGAAAFIARC RVAPLRGTGA ALSPFNAFLI LQGLETLALR MERHTENARK
VAEFLGTHPQ VSWVKYAGLP NHPEHALAMK YMGGKPASIM SFGIKGGVAA GSRFIDALKL
IVRLVNIGDA KSLACHPAST THRQLNDQEL AQAGVSRDMI RLSIGIEHID DILEDLKQAL
DATI
//
