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Database: UniProt
Entry: A0A3S0PSV3_9FLAO
LinkDB: A0A3S0PSV3_9FLAO
Original site: A0A3S0PSV3_9FLAO 
ID   A0A3S0PSV3_9FLAO        Unreviewed;       390 AA.
AC   A0A3S0PSV3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=O-succinylhomoserine sulfhydrylase {ECO:0000256|HAMAP-Rule:MF_02056};
DE            Short=OSH sulfhydrylase {ECO:0000256|HAMAP-Rule:MF_02056};
DE            Short=OSHS sulfhydrylase {ECO:0000256|HAMAP-Rule:MF_02056};
DE            EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_02056};
GN   Name=metZ {ECO:0000256|HAMAP-Rule:MF_02056};
GN   ORFNames=EKM02_05795 {ECO:0000313|EMBL:RTZ01512.1};
OS   Flavobacterium sp. RSP49.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2497487 {ECO:0000313|EMBL:RTZ01512.1, ECO:0000313|Proteomes:UP000272024};
RN   [1] {ECO:0000313|EMBL:RTZ01512.1, ECO:0000313|Proteomes:UP000272024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSP49 {ECO:0000313|EMBL:RTZ01512.1,
RC   ECO:0000313|Proteomes:UP000272024};
RA   Liu Q., Xin Y.-H.;
RT   "Flavobacterium sp. nov., isolated from glacier ice.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of L-homocysteine from O-succinyl-L-
CC       homoserine (OSHS) and hydrogen sulfide. {ECO:0000256|HAMAP-
CC       Rule:MF_02056}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + O-succinyl-L-homoserine = L-homocysteine +
CC         succinate; Xref=Rhea:RHEA:27826, ChEBI:CHEBI:29919,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:57661, ChEBI:CHEBI:58199;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02056};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_02056, ECO:0000256|RuleBase:RU362118};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homocysteine from O-succinyl-L-homoserine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_02056}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_02056}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family. MetZ
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_02056}.
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:RTZ01512.1}.
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DR   EMBL; RYDN01000007; RTZ01512.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S0PSV3; -.
DR   UniPathway; UPA00051; UER00449.
DR   Proteomes; UP000272024; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0071268; P:homocysteine biosynthetic process; 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   HAMAP; MF_02056; MetZ; 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR006234; O-succ-hSer_sulfhydrylase.
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   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW   Aminotransferase {ECO:0000313|EMBL:RTZ01512.1};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_02056};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02056, ECO:0000313|EMBL:RTZ01512.1}.
FT   MOD_RES         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02056,
FT                   ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   390 AA;  43231 MW;  8BCBEF653B6A4CCD CRC64;
     MNDQEFGFET SAIRTQLERT QYLEHSVPLY LTSSFVFEDA EDMRASFAEE KDRNIYSRYS
     NPNTNEFVDK VCIMEGAAAG FAFASGMAAV YSTLAALLKS GDHIVSSSSV FGATHSLFIN
     YFPKWNIETS YFDINKPETI ESFITPNTKI LFAESPTNPA VDIIDLELLG TIAKKHNLIL
     VIDNCFATPY LQQPIKWGAH LVVHSATKLM DGQGRVLGGI TVGDAELIQK IYLFSRLTGP
     SLSPFNAWVL SKSLETLAIR LDRHCENAMK VAEFLEQHPN VNRVKYPFLK SHPQYEIAQK
     QMKLGGNIVA FEIKGGLEAG RNFLDKIKLC SLSPNLGDTR TIVTHPASTT HSKLSVEERL
     SVSITDGLVR VSVGLETVKD VIADLEQALS
//
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