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Entry: U5WVF9_MYCKA
LinkDB: U5WVF9_MYCKA
Original site: U5WVF9_MYCKA 
ID   U5WVF9_MYCKA            Unreviewed;       409 AA.
AC   U5WVF9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
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=MKAN_17720 {ECO:0000313|EMBL:AGZ51916.1};
OS   Mycobacterium kansasii ATCC 12478.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=557599 {ECO:0000313|EMBL:AGZ51916.1, ECO:0000313|Proteomes:UP000017786};
RN   [1] {ECO:0000313|EMBL:AGZ51916.1, ECO:0000313|Proteomes:UP000017786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12478 {ECO:0000313|EMBL:AGZ51916.1,
RC   ECO:0000313|Proteomes:UP000017786};
RG   McGill University Mycobacterium genome consortium;
RA   Veyrier F.J., Behr M.A.;
RT   "Genome sequence of Mycobacterium kansasii.";
RL   Submitted (OCT-2013) 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|ARBA:ARBA00011881,
CC       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; CP006835; AGZ51916.1; -; Genomic_DNA.
DR   RefSeq; WP_023370162.1; NC_022663.1.
DR   AlphaFoldDB; U5WVF9; -.
DR   GeneID; 29700062; -.
DR   KEGG; mkn:MKAN_17720; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_0_11; -.
DR   OrthoDB; 9780685at2; -.
DR   UniPathway; UPA00051; UER00449.
DR   Proteomes; UP000017786; Chromosome.
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|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW   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         222
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02056,
FT                   ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   409 AA;  43225 MW;  6787EEFB7233CEBF CRC64;
     MTDHPAIRTP KVLPDGVGQA TIGVRGGLLR SGFDETAEAM YLTSGYVYES AAAAEQSFSG
     ELDHFVYSRY GNPTVAMFEE RLRLIEGAPA AFATASGMAA VFTSLGALLA AGDRLVAARS
     LFGSCFVVCN EILPRWGVET VFVDGDDLSQ WEQALADPSK PTRAVFFETP ANPMQSLVDI
     AAVTELAHAA GAKVVLDNVF ATPLLQQGFP LGVDVVVYSG TKHIDGQGRV LGGAILGDKE
     YIDGPVQKLM RHTGPAMSAF NAWVLLKGLE TLAVRVECSN SSALRIAAFL EAHPAVSWVR
     YPFLPSHPQY NLAKRQMSGG GTVVTFALDA PESAAKQRAF EVLDKLALID ISNNLGDAKS
     LVTHPATTTH RAMGPEGRAA IGLGDGVVRI SVGLEGADDL IADLDRALG
//
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