ID A0A522MHB9_9BURK Unreviewed; 404 AA. AC A0A522MHB9; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 02-DEC-2020, entry version 8. 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=EPN61_01265 {ECO:0000313|EMBL:TAM51808.1}; OS Burkholderiaceae bacterium. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae. OX NCBI_TaxID=2030806 {ECO:0000313|EMBL:TAM51808.1, ECO:0000313|Proteomes:UP000316036}; RN [1] {ECO:0000313|EMBL:TAM51808.1, ECO:0000313|Proteomes:UP000316036} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FW106-02_bin.10 {ECO:0000313|EMBL:TAM51808.1}; RA Tian R., Ning D., He Z., Zhang P., Shi W., Wu L., Zhang Y., Yang Y., RA Arkin A., Matthew F., Hazen T., Stalh D., Alm E., Zhou J.; RT "Small is mighty: adaptation of Patescibacteria to groundwater environment RT leads to their genome simplicity."; RL Submitted (JAN-2019) 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:TAM51808.1}. 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; SCRR01000041; TAM51808.1; -; Genomic_DNA. DR UniPathway; UPA00051; UER00449. DR Proteomes; UP000316036; 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; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 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; IPR015422; PyrdxlP-dep_Trfase_dom1. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR PANTHER; PTHR11808; PTHR11808; 1. DR Pfam; PF01053; Cys_Met_Meta_PP; 1. DR PIRSF; PIRSF001434; CGS; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01325; O_suc_HS_sulf; 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, ECO:0000256|PIRSR:PIRSR001434-2, KW ECO:0000256|RuleBase:RU362118}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_02056}. FT MOD_RES 212 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02056, FT ECO:0000256|PIRSR:PIRSR001434-2" SQ SEQUENCE 404 AA; 43058 MW; 39522D74BFC0AF96 CRC64; MTERALPPDL HPETLAVRVA VDKSQYGENS ESLYLTSSFI QSDAETAVRR FAGEEEGFTY SRFTNPTVAS MEQRLAALEG TEACVGTSSG MAAILLLCMG LLKAGDHVIC SQSVFGSTMK LIGGEFGKFG VQTTFVSQTD VAQWRAAIQP NTRLLFAETP TNPLTDVCDI QSLADVAHAA GALLAVDNCF CSPALQQPVK FGADLIIHSG TKYLDGQGRV MAGAVCGPHH LIEEKLVPVL RSAGMTLSAF NAWIVLKGME TLSIRMQAQS TSALALASWL EVQPAIACVH YSGLKSHPQH ELAMRQQSGL GGAVVSFDVK GATPEEARRN AFHLIDSTRV CSITANLGDT KTTITHPAST SHGRLTEEQR QAAGIGQGLI RLAVGLEHID DLKADLARGL DTLP //