ID W7DSI3_9PROT Unreviewed; 400 AA.
AC W7DSI3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=COMX_07795 {ECO:0000313|EMBL:EUK17880.1};
OS Commensalibacter papalotli (ex Servin-Garciduenas et al. 2014).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1208583 {ECO:0000313|EMBL:EUK17880.1, ECO:0000313|Proteomes:UP000019250};
RN [1] {ECO:0000313|EMBL:EUK17880.1, ECO:0000313|Proteomes:UP000019250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX-MONARCH01 {ECO:0000313|Proteomes:UP000019250};
RX PubMed=24604647;
RA Servin-Garciduenas L.E., Sanchez-Quinto A., Martinez-Romero E.;
RT "Draft Genome Sequence of Commensalibacter papalotli MX01, a Symbiont
RT Identified from the Guts of Overwintering Monarch Butterflies.";
RL Genome Announc. 2:e00128-14(2014).
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:EUK17880.1}.
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DR EMBL; ATSX01000002; EUK17880.1; -; Genomic_DNA.
DR RefSeq; WP_034339655.1; NZ_ATSX01000002.1.
DR AlphaFoldDB; W7DSI3; -.
DR STRING; 1208583.COMX_07795; -.
DR PATRIC; fig|1208583.4.peg.1569; -.
DR eggNOG; COG0626; Bacteria.
DR OrthoDB; 9790858at2; -.
DR UniPathway; UPA00051; UER00449.
DR Proteomes; UP000019250; 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:UP000019250};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02056}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02056,
FT ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 400 AA; 43986 MW; 9C321C1B2A3F3F96 CRC64;
MKRAKTYRPA TQLIHGGVER TSFDETSDAV FLTSGFIYDS AEQAERTFTG EEDRYQYSRF
NNPNLTSLQN RLSILENAEA CVLTSTGMSA IYASLMPLIK TGDRVVASRA LFGSSYWIVE
NLLPKLGIET VFVDGTKLDQ WQEALSKPTA AVLIETPSNP MLDILDIKAI ADLTHKAGGK
LIVDNVFATP LYQHPLQWGA DIVVYSCTKH IDGQGRVLGG AVLGNKETIE DNITPFVRNT
GISLSPFNAW VLFKGLETLP LRVEKMTQNA QACSEFLEKS PLISRVLYPG LKSHPHYELG
QKQMSASSTM IGFEIKGGKK AAFTFMNALE LILISNNLGD NRCIMTHPAT TTHMKIGEKE
RLHLGITDGS IRFSVGIEDV QDIIEDLQRG LDAVAALSPS
//
