ID A0A163DM07_9NEIS Unreviewed; 395 AA.
AC A0A163DM07;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=AVW16_05630 {ECO:0000313|EMBL:KZE34961.1};
OS Crenobacter luteus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Crenobacter.
OX NCBI_TaxID=1452487 {ECO:0000313|EMBL:KZE34961.1, ECO:0000313|Proteomes:UP000076625};
RN [1] {ECO:0000313|Proteomes:UP000076625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN10 {ECO:0000313|Proteomes:UP000076625};
RA Hong K.W.;
RT "Draft genome of Chromobacterium sp. F49.";
RL Submitted (JAN-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:KZE34961.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LQQU01000004; KZE34961.1; -; Genomic_DNA.
DR RefSeq; WP_066609827.1; NZ_LQQU01000004.1.
DR AlphaFoldDB; A0A163DM07; -.
DR STRING; 1452487.AVW16_05630; -.
DR OrthoDB; 9805807at2; -.
DR UniPathway; UPA00051; UER00449.
DR Proteomes; UP000076625; 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:UP000076625};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02056}.
FT MOD_RES 213
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02056,
FT ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 395 AA; 42401 MW; A3910282CC5926E7 CRC64;
MTQHTDPSAK LRPETLAIRA GREISDYREH SQALFLTSSF TYDTAAEAAA MFIGEQDGYI
YSRFTNPTVA AFQQRLAALE GGERAIATAS GMAAIQATML TLLKAGDHIV SSQSLFGSTI
NLFNGILAKF GVEVSYVDAT DLDAWRAATR PNTRVFFLET PSNPLTELSD IAAVADIAHA
AGALLVVDNC FCTPVLQQPL KLGADLVVHS ATKSLDGHGR VLGGAVVGSD KLIEPIYLHV
RTAGPSLSAF NAWTLLSGLE TLFVRVERQC ETALEIARWL EAQPQVERVF YPGLESHPQH
ALAQRQQAAG GTVVSFVLKG GRDAAWRLID GVEVFSRTSN LGDVKSTVTH PASTTHARIT
PEARARAGIV EGLVRLAIGL EHVEDLKADL AARFA
//
