ID A0A0M6XN29_9RHOB Unreviewed; 397 AA.
AC A0A0M6XN29;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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:CTQ32338.1};
GN ORFNames=JAN5088_01103 {ECO:0000313|EMBL:CTQ32338.1};
OS Jannaschia rubra.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=282197 {ECO:0000313|EMBL:CTQ32338.1, ECO:0000313|Proteomes:UP000048908};
RN [1] {ECO:0000313|EMBL:CTQ32338.1, ECO:0000313|Proteomes:UP000048908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5088 {ECO:0000313|EMBL:CTQ32338.1,
RC ECO:0000313|Proteomes:UP000048908};
RA Noorani M.;
RL Submitted (JUL-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; CXPG01000013; CTQ32338.1; -; Genomic_DNA.
DR RefSeq; WP_055681792.1; NZ_FOOS01000005.1.
DR AlphaFoldDB; A0A0M6XN29; -.
DR STRING; 282197.SAMN04488517_105101; -.
DR OrthoDB; 9805807at2; -.
DR UniPathway; UPA00051; UER00449.
DR Proteomes; UP000048908; 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:UP000048908};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02056, ECO:0000313|EMBL:CTQ32338.1}.
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02056,
FT ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 397 AA; 42884 MW; 3E33D4877AAF8142 CRC64;
MKDSSPRARK PRTLAVHAGT RRSQYGEVSE AMFLTQGFVY ETAEIAEARF QHSTRDEFIY
ARYGNPTVAM FEDRMAALEG TEDAFATASG MAAVNGALVS MLRAGDHVVA SRALFGSCLY
ILDEILPRFG VEVTLVDGTD LSAWKAAIRP DTKCVFFESV SNPALEVIDI RGVSDLAHAV
GATVIVDNVF VTPTYSRALD LGADVVVYST TKHIDGQGRC LGGVICGTTE FVRKVAEPYL
KHTGAAMSPF NAWVMLKGLE HMDLRVRAQA ETCERLAIAV EGHPKLARVI HPHLISHPQQ
ALARKQMEKG GTVLALDLAG GKEAAFRFLN ALEIVLISNN LGDAKSIVTH PATTTHQRLP
EEQKAELGIT PGLVRLSCGL EDADDLIADV LSALDQA
//
