ID F2I3U6_PELSM Unreviewed; 432 AA.
AC F2I3U6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=O-acetylhomoserine sulfhydrylase / O-succinylhomoserine sulfhydrylase {ECO:0000313|EMBL:AEA80746.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:AEA80746.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:AEA80746.1};
GN OrderedLocusNames=SAR11G3_00271 {ECO:0000313|EMBL:AEA80746.1};
OS Pelagibacter sp. (strain IMCC9063).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=1002672 {ECO:0000313|EMBL:AEA80746.1, ECO:0000313|Proteomes:UP000009181};
RN [1] {ECO:0000313|EMBL:AEA80746.1, ECO:0000313|Proteomes:UP000009181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC9063 {ECO:0000313|EMBL:AEA80746.1,
RC ECO:0000313|Proteomes:UP000009181};
RX PubMed=21515764; DOI=10.1128/JB.05033-11;
RA Oh H.M., Kang I., Lee K., Jang Y., Lim S.I., Cho J.C.;
RT "Complete genome sequence of strain IMCC9063, belonging to SAR11 subgroup
RT 3, isolated from the Arctic Ocean.";
RL J. Bacteriol. 193:3379-3380(2011).
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; CP002511; AEA80746.1; -; Genomic_DNA.
DR RefSeq; WP_013694911.1; NC_015380.1.
DR AlphaFoldDB; F2I3U6; -.
DR STRING; 1002672.SAR11G3_00271; -.
DR KEGG; pel:SAR11G3_00271; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_2_5; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000009181; Chromosome.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009181};
KW Transferase {ECO:0000313|EMBL:AEA80746.1}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 432 AA; 46744 MW; D33443B7B82AA91A CRC64;
MTTTSKHPET ISLHGGTYRR DESTTAVAVP IYQTTSYQFN SAEHAENLFG LKEFGNIYTR
IGNPTTNVLE ERVAALEGGV AAVCVSSGQA ASAFVVQNLC STGDNIVAST DLYGGTVNLF
NNTLKSMGIE VRYADPKDPE SFAKATDKKT RLYYAETLPN PSLRVFPIKE VSDIGRKLGI
PLVMDNTACP VICKPIDHGA AIVMHSLTKF IGGHGTTIGG IIVDAGNFDW SIDKERQPNI
WQPDASYHGA VWGDAVPVLT GANIPYIIRA RVVLLRDLGS AISPTSAWQI IQGLETVTLR
MKQHCENAEK VKNFLLKHKK IEKVIYSTLH EGEIGERTKK YFKGGNGALM GIEVKGGKEA
GKKFIDSLKL LYHVANIGDA RSLAIHPAST THSQLSEKDL LAAGVTPGYV RLSIGIEHAD
DIIADIDQAL NA
//
