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Database: UniProt
Entry: A0A1D9B9W4_9NEIS
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ID   A0A1D9B9W4_9NEIS        Unreviewed;       391 AA.
AC   A0A1D9B9W4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=BJP62_01280 {ECO:0000313|EMBL:AOX99203.1};
OS   Jeongeupia sp. USM3.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Jeongeupia.
OX   NCBI_TaxID=1906741 {ECO:0000313|EMBL:AOX99203.1, ECO:0000313|Proteomes:UP000176825};
RN   [1] {ECO:0000313|EMBL:AOX99203.1, ECO:0000313|Proteomes:UP000176825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USM3 {ECO:0000313|EMBL:AOX99203.1,
RC   ECO:0000313|Proteomes:UP000176825};
RA   Kho H.P.;
RT   "Jeongeupia sp. strain USM3 Genome sequencing and assembly.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOX99203.1, ECO:0000313|Proteomes:UP000176825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USM3 {ECO:0000313|EMBL:AOX99203.1,
RC   ECO:0000313|Proteomes:UP000176825};
RA   de Groot N.N.;
RL   Submitted (OCT-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; CP017668; AOX99203.1; -; Genomic_DNA.
DR   RefSeq; WP_070525736.1; NZ_CP017668.1.
DR   AlphaFoldDB; A0A1D9B9W4; -.
DR   STRING; 1906741.BJP62_01280; -.
DR   KEGG; jeu:BJP62_01280; -.
DR   OrthoDB; 9805807at2; -.
DR   UniPathway; UPA00051; UER00449.
DR   Proteomes; UP000176825; 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;  41654 MW;  3111E74D9B0ABBA5 CRC64;
     MTDRTDLHPD TLAVRAGTHR TEFGEHSDAL FLTSSFVVDS AEDAALKFGG QIPGYTYSRF
     TNPTVTAFED RLAALEGAER AVATASGMSA ILGLCMAHLK AGDHILASAG LFGSTIQFFN
     NYMSKFGVEV SYAKPTDPAD WAALVRPNTR LFFLETPSNP LTDVSDIGAI AEIAHANGAL
     LAVDNCFCSP ILQQPLALGA DIVIHSATKY LDGQGRVLGG AVVGKSEVVE PVYLFLRTSG
     PTLSAFNAWV LLKGMETLPL RMRAHCDNAF KLATWLEAQP AVERVYYPGL ESHPQHALAM
     RQQKGGGGVV SFELKGGKDA AWKLVDAVQL MSRTANLGDV RTTITHPAST THGRLTPEAR
     AAAGIRDGLI RIAVGLEHID DLTADLALGL G
//
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