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Entry: A0A2T4JKH8_9RHOB
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ID   A0A2T4JKH8_9RHOB        Unreviewed;       391 AA.
AC   A0A2T4JKH8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, 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   ECO:0000313|EMBL:PTE18419.1};
GN   ORFNames=C5F46_04490 {ECO:0000313|EMBL:PTE18419.1};
OS   Phaeovulum veldkampii DSM 11550.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Phaeovulum.
OX   NCBI_TaxID=1185920 {ECO:0000313|EMBL:PTE18419.1, ECO:0000313|Proteomes:UP000241899};
RN   [1] {ECO:0000313|EMBL:PTE18419.1, ECO:0000313|Proteomes:UP000241899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11550 {ECO:0000313|EMBL:PTE18419.1,
RC   ECO:0000313|Proteomes:UP000241899};
RA   Meyer T.E., Miller S., Lodha T., Gandham S., Chintalapati S.,
RA   Chintalapati V.R.;
RT   "Rhodobacter veldkampii.";
RL   Submitted (MAR-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:PTE18419.1}.
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DR   EMBL; PZKF01000007; PTE18419.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4JKH8; -.
DR   OrthoDB; 9805807at2; -.
DR   UniPathway; UPA00051; UER00449.
DR   Proteomes; UP000241899; Unassembled WGS sequence.
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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000241899};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02056}.
FT   MOD_RES         206
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02056,
FT                   ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   391 AA;  41459 MW;  0B30A6273D4F9A8D CRC64;
     MDEWQAGTKL VHSGIRRSQY GEMSEALFLT QGYVYATAEA AEARFEALGE DEFIYSRYAN
     PTTRMFEERL AAVEGTQDAF ATASGMAAVH GVLVSVLKAG DHVVAARALF GSCLIVLDMF
     RRFGVEVTLV DGRDLDAWRA AVRPGTRAVF FESVSNPTLE VIDIKAVAEI AHAAGALVIV
     DNVFATPVGS RATEMGADLV IYSATKHIDG GGRVLGGVIC GSADLIRGTV EPCLKHLGPS
     ISPFNAWVML KGMETLALRV RAMTASAQAL AQAVEGHPAL ARTIYPGLAS HPQHALALEQ
     MRHGGTIVAL DLAGGKAAAF RFLNALRVFT LSNNLGDAKS IATHPATTTH QRLPADQKVT
     LGITPGLVRL SLGIEDAADI VADVTRALDM I
//
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