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Database: UniProt
Entry: A0A3D9HLU5_9FLAO
LinkDB: A0A3D9HLU5_9FLAO
Original site: A0A3D9HLU5_9FLAO 
ID   A0A3D9HLU5_9FLAO        Unreviewed;       391 AA.
AC   A0A3D9HLU5;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=O-succinylhomoserine sulfhydrylase {ECO:0000313|EMBL:RED50301.1};
GN   ORFNames=DFQ02_101328 {ECO:0000313|EMBL:RED50301.1};
OS   Seonamhaeicola aphaedonensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1461338 {ECO:0000313|EMBL:RED50301.1, ECO:0000313|Proteomes:UP000256629};
RN   [1] {ECO:0000313|EMBL:RED50301.1, ECO:0000313|Proteomes:UP000256629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8487 {ECO:0000313|EMBL:RED50301.1,
RC   ECO:0000313|Proteomes:UP000256629};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUL-2018) 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|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:RED50301.1}.
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DR   EMBL; QRDX01000001; RED50301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9HLU5; -.
DR   OrthoDB; 9803729at2; -.
DR   Proteomes; UP000256629; Unassembled WGS sequence.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808:SF90; CYSTATHIONINE GAMMA-LYASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 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:UP000256629}.
FT   MOD_RES         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   391 AA;  43267 MW;  EA8AB40AE8D9BD85 CRC64;
     MSKEKKHFET EAVRTQSETT QFSEHSVPLY LTSGFVFDDA EEMRASFAEE KQRDLYSRYS
     NPNVNEFVEK VCKMEGAEAG FAFASGMAAV FSTFATLLNA GDHVVSCSSV FGATHGLFTK
     YFPKWNIECS YFNINEVETV ESLIKPNTKF IYAETPTNPG VDVLDLEYLS GICKKHNLLL
     VIDNCFATPY LQNPIKFGAD LVIHSATKLM DGQGRVLGGI TVGNKALIRE IYLFSRLTGP
     AMSPFNAWVL SKSLETLAIR VEKHCENALK LAEYLEKHPK VKWVKYPFLK SHSKYAVAKK
     QMRLGGNIVA FEVEGGLEGG RSFFDNIKMC SLSANLGDSR TIVTHPASTT HAKVEPEVKA
     AAGITNGMVR CSLGLEHIDD IIADIEQALN S
//
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