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Database: UniProt
Entry: A0A3Q9FNT3_9BACT
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ID   A0A3Q9FNT3_9BACT        Unreviewed;       391 AA.
AC   A0A3Q9FNT3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=EI427_11890 {ECO:0000313|EMBL:AZQ62912.1};
OS   Flammeovirga pectinis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Flammeovirga.
OX   NCBI_TaxID=2494373 {ECO:0000313|EMBL:AZQ62912.1, ECO:0000313|Proteomes:UP000267268};
RN   [1] {ECO:0000313|EMBL:AZQ62912.1, ECO:0000313|Proteomes:UP000267268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L12M1 {ECO:0000313|EMBL:AZQ62912.1,
RC   ECO:0000313|Proteomes:UP000267268};
RA   Bae J.-W., Jeong Y.-S., Kang W.;
RT   "Flammeovirga pectinis sp. nov., isolated from the gut of the Korean
RT   scallop, Patinopecten yessoensis.";
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}.
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DR   EMBL; CP034562; AZQ62912.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q9FNT3; -.
DR   KEGG; fll:EI427_11890; -.
DR   OrthoDB; 9803729at2; -.
DR   UniPathway; UPA00051; UER00449.
DR   Proteomes; UP000267268; Chromosome 1.
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:AZQ62912.1};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_02056}; Reference proteome {ECO:0000313|Proteomes:UP000267268};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02056, ECO:0000313|EMBL:AZQ62912.1}.
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   391 AA;  42930 MW;  EA1039996D0962F6 CRC64;
     MSQEDKKFET IAVRAQTERS HNREHSVPIY ATSSFTFEDA DHASALFSDE VEGNIYSRYS
     NPNNDEFIDK LVQLEGAEAG IATSSGMSAM FLSIASFVKS GDHVVASRSL FGSTHQILTQ
     LLPRWGVSHT YVDFDDLEGF DKAVQPNTKM IFIETPSNPA IDLIDIEALA KIANKHNVIL
     NVDNCFATPY IQNPIALGAH IVTHSATKFI DGQGRVLAGA ILGTKEHMNE VKFLSRHTGP
     ALSPFHGWIL SKSLETLAVR MDKHCDNALK VAKALEGFPQ VQMVKYPFLK SHPQYDLAKK
     QMRLGGAIVS FEIKGGVEAG KKFWDSLNMI SRSSNLGDTR TIATHPASTT HSKLSEEERL
     SVGITPGLIR ISVGLEHLDD IIGDIKQALE A
//
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