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Database: UniProt
Entry: A0A0C3RCG0_9PROT
LinkDB: A0A0C3RCG0_9PROT
Original site: A0A0C3RCG0_9PROT 
ID   A0A0C3RCG0_9PROT        Unreviewed;       393 AA.
AC   A0A0C3RCG0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=SQ11_08430 {ECO:0000313|EMBL:KIO49045.1};
OS   Nitrosospira sp. NpAV.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=58133 {ECO:0000313|EMBL:KIO49045.1, ECO:0000313|Proteomes:UP000031969};
RN   [1] {ECO:0000313|EMBL:KIO49045.1, ECO:0000313|Proteomes:UP000031969}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NpAV {ECO:0000313|EMBL:KIO49045.1,
RC   ECO:0000313|Proteomes:UP000031969};
RA   Rice M.C., Lim C.K., Sayavedra-Soto L.A., Norton J.M., Klotz M.G.;
RT   "Nitrosospira sp. NpAV genome sequencing.";
RL   Submitted (JAN-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}.
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:KIO49045.1}.
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DR   EMBL; JXQM01000012; KIO49045.1; -; Genomic_DNA.
DR   RefSeq; WP_041513720.1; NZ_JXQM01000012.1.
DR   AlphaFoldDB; A0A0C3RCG0; -.
DR   OrthoDB; 9805807at2; -.
DR   UniPathway; UPA00051; UER00449.
DR   Proteomes; UP000031969; 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.
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         207
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02056,
FT                   ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   393 AA;  41879 MW;  3272AE7D2110BA8C CRC64;
     MSDDFELETL ALHTGIHRSQ FNEHSEALYL TSSFVFDSAA QAAARFSGAE PGNIYSRFTN
     PTVTAFEERL AALEGAEACV ATSSGMSAIL ACVMGLLSAG DHIVASRSLF GSTVNLFNTI
     LKRFNIETTF VSATDISAWE AAIKPATKLL FIETPSNPLT EISDIATLAA VAKKAGAWLA
     VDNCFCSPAL QRPLDLGADL VIHSATKYLE GQGRVLGGAV LGKRDLVMEQ GVFGFLRTAG
     PSLSPFNAWV ILKGMETLKI RMEAHCANAL QIARWLEAQP GVARVHYPGL PSHPQHALAK
     RQQKAGGGIV SFELKNGKEA AWRVVDSVRL ISITANLGDT KSTLTHPATT THARISQENR
     DAAGITDGLL RIAVGLEAVK DLKADLARGL NAS
//
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