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Database: UniProt
Entry: A0A136H240_9GAMM
LinkDB: A0A136H240_9GAMM
Original site: A0A136H240_9GAMM 
ID   A0A136H240_9GAMM        Unreviewed;       396 AA.
AC   A0A136H240;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=AXW16_02210 {ECO:0000313|EMBL:KXJ49773.1};
OS   Cycloclasticus sp. Phe_18.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Cycloclasticus.
OX   NCBI_TaxID=1795870 {ECO:0000313|EMBL:KXJ49773.1, ECO:0000313|Proteomes:UP000070359};
RN   [1] {ECO:0000313|Proteomes:UP000070359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Donaho J.A., Gutierrez T., Seitz K.W., Teske A.P.,
RA   Baker B.J.;
RL   Submitted (FEB-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}.
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:KXJ49773.1}.
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DR   EMBL; LSMQ01000015; KXJ49773.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136H240; -.
DR   UniPathway; UPA00051; UER00449.
DR   Proteomes; UP000070359; 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         211
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02056,
FT                   ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   396 AA;  43221 MW;  55E6EA757A033A81 CRC64;
     MSDIDWQDYS IETQGIRAGQ HRTPENEHSD AIFPTSSYVF ESAQDAFERF SGKSEGNIYS
     RFTNPTVRAF EQRLAVMEGA ERAMATSSGM AAINVVCLGL LSAGDHVICS RSVFGNTALM
     FKNIMQKFAV ETTFVDLDDI NAWSAAIKPN TRFLFLETPS NPLGNVADIK KLAELAHAND
     ALVIVDNVYC TPALQKPLSL GADLVVHSAT KYIDGQGRCI GGAVVGNNAL IEEKIYPILR
     TAGHTMSPFN AWVFHKGLET LSLRMEKHCS NALIVAQWLE QQPMVEKVYY TGLPSHPQHE
     LAKQQQTGFG GIVSFEVKGG KENAWKVVDA TQMISITANL GDVKSMITHP STTTHGRLTE
     EERSKAGITD SLLRLGVGLE NVADITADLD RGLSSL
//
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