ID A0A0P1I5M6_9RHOB Unreviewed; 396 AA.
AC A0A0P1I5M6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:CUJ91825.1};
GN ORFNames=RUE5091_01146 {ECO:0000313|EMBL:CUJ91825.1};
OS Ruegeria denitrificans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1715692 {ECO:0000313|EMBL:CUJ91825.1, ECO:0000313|Proteomes:UP000051260};
RN [1] {ECO:0000313|EMBL:CUJ91825.1, ECO:0000313|Proteomes:UP000051260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5091 {ECO:0000313|EMBL:CUJ91825.1,
RC ECO:0000313|Proteomes:UP000051260};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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; CYUD01000003; CUJ91825.1; -; Genomic_DNA.
DR RefSeq; WP_058280903.1; NZ_CYUD01000003.1.
DR AlphaFoldDB; A0A0P1I5M6; -.
DR STRING; 1715692.RUE5091_01146; -.
DR OrthoDB; 9805807at2; -.
DR UniPathway; UPA00051; UER00449.
DR Proteomes; UP000051260; 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};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02056, ECO:0000313|EMBL:CUJ91825.1}.
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 396 AA; 42390 MW; 0CCD83096209F9B8 CRC64;
MSESWKKRTQ AVHGGIRRSQ YNEVSEAIFL TQGFVYDNAE QAEARFLECG PDDFIYARYG
NPTVSMFEQR IAALEGGEDA FATASGMAAV NGALTSILKA GDHIVSAKAL FGSCLYIVET
ILTRFGVDVT YVDGTDLEQW KAAIRTDTKA VFFESMSNPT LEVIDIASVA ELAHAAGALV
IVDNVFSTPV FSRAIEQGAD VVIYSATKHI DGQGRALGGV IIGTKDFIRG TVEPYMKHTG
GALSPFNAWI MLKGIETMTL RVNAQAETAQ ILAEALEGHA ALERTLYPGL KTHPQNALVQ
SQLGGKGGTV LALDINGGKK AAFAFLNALT IPVISNNLGD TKSIATHPAT TTHQRLSDEQ
KDELSITPGL IRLSIGLEDS GDLLADIKQA LDVSQR
//
