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Database: UniProt
Entry: A0A0X8GN79_9BURK
LinkDB: A0A0X8GN79_9BURK
Original site: A0A0X8GN79_9BURK 
ID   A0A0X8GN79_9BURK        Unreviewed;       391 AA.
AC   A0A0X8GN79;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=VN23_06780 {ECO:0000313|EMBL:AMC34324.1};
OS   Janthinobacterium sp. B9-8.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1236179 {ECO:0000313|EMBL:AMC34324.1, ECO:0000313|Proteomes:UP000069577};
RN   [1] {ECO:0000313|EMBL:AMC34324.1, ECO:0000313|Proteomes:UP000069577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B9-8 {ECO:0000313|EMBL:AMC34324.1,
RC   ECO:0000313|Proteomes:UP000069577};
RA   Xu X., Jin W., Wu Q., Jiang L., Huang H.;
RT   "The whole genome sequence of Janthinbacterium sp. B9-8, a bacterium
RT   isolated from low temperature sewage.";
RL   Submitted (JAN-2016) 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; CP014222; AMC34324.1; -; Genomic_DNA.
DR   RefSeq; WP_046351890.1; NZ_CP014222.1.
DR   AlphaFoldDB; A0A0X8GN79; -.
DR   STRING; 1236179.VN23_06780; -.
DR   KEGG; jab:VN23_06780; -.
DR   OrthoDB; 9805807at2; -.
DR   UniPathway; UPA00051; UER00449.
DR   Proteomes; UP000069577; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
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   NCBIfam; TIGR01325; O_suc_HS_sulf; 1.
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.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_02056}; Transferase {ECO:0000256|HAMAP-Rule:MF_02056}.
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02056,
FT                   ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   391 AA;  41741 MW;  556BDC35AF9A79C6 CRC64;
     MFEDEFLHPD TLAVRAGTTR SQFGEHSDAM YLTSSFVVGS AEEASLKFTG QIPGFIYSRF
     TNPTVSAFEE RLAALEGAER AVATASGMSA ILSLFMAHLK SGDHVVASAS LFGSTIQLLN
     VYLSKFGVSV TYVSATDTAE WADACQPNTK LLFLETPSNP LTEISDIRTI ADIAHAHDAL
     LVVDNCFCTP ILQKPLALGA DLVVHSATKY IDGQGRVLGG AVVGSSVLVE PVYLFLRTAG
     PSLSAFNAWV LLKGLETLPI RMRAHSETAL KLATYLEAHP AIEQVYYPGL PSHPQHALAM
     TQQNAGGGMV SFVVKGGREQ AWKIVDAVQL ISRTANLGDT RSTITHPAST THARITPAAR
     EAAGITEGLI RISVGLEYID DLIADLEQGL A
//
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