(data stored in ACNUC7421 zone)

SWISSPROT: Q13S17_PARXL

ID   Q13S17_PARXL            Unreviewed;       396 AA.
AC   Q13S17;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 84.
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=Bxe_B2873 {ECO:0000313|EMBL:ABE33122.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33122.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33122.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33122.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the formation of L-homocysteine from O-
CC       succinyl-L-homoserine (OSHS) and hydrogen sulfide.
CC       {ECO:0000256|HAMAP-Rule:MF_02056}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + O-succinyl-L-homoserine = L-
CC         homocysteine + succinate; Xref=Rhea:RHEA:27826,
CC         ChEBI:CHEBI:29919, ChEBI:CHEBI:30031, ChEBI:CHEBI:57661,
CC         ChEBI:CHEBI:58199; Evidence={ECO:0000256|HAMAP-Rule:MF_02056};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02056,
CC         ECO:0000256|RuleBase:RU362118};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homocysteine from O-succinyl-L-homoserine: step
CC       1/1. {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}.
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DR   EMBL; CP000271; ABE33122.1; -; Genomic_DNA.
DR   RefSeq; WP_011490503.1; NZ_CP008762.1.
DR   STRING; 266265.Bxe_B2873; -.
DR   EnsemblBacteria; ABE33122; ABE33122; Bxe_B2873.
DR   GeneID; 4006762; -.
DR   KEGG; bxb:DR64_5203; -.
DR   KEGG; bxe:Bxe_B2873; -.
DR   PATRIC; fig|266265.5.peg.4817; -.
DR   eggNOG; ENOG4105C28; Bacteria.
DR   eggNOG; COG0626; LUCA.
DR   HOGENOM; HOG000246417; -.
DR   KO; K10764; -.
DR   OMA; AVDNCFC; -.
DR   OrthoDB; 637281at2; -.
DR   BioCyc; BXEN266265:BXE_RS22830-MONOMER; -.
DR   UniPathway; UPA00051; UER00449.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   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;
DR   PRODOM; Q13S17.
DR   SWISS-2DPAGE; Q13S17.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Lyase {ECO:0000313|EMBL:ABE33122.1};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02056,
KW   ECO:0000256|PIRSR:PIRSR001434-2, ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02056}.
FT   MOD_RES     207    207       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02056,
FT                                ECO:0000256|PIRSR:PIRSR001434-2}.
SQ   SEQUENCE   396 AA;  42586 MW;  7725486AC73558C2 CRC64;
     MDDSLNFDTL AVRSGTVRSD FNEHSEAIFL TSSFVFASAA DAAEKFRNSE DNYTYSRFTN
     PTVSMFQDRL AALEGGEACM ATASGMAAIM SVVMSALQAG DHLVSSQALF GSTLGMFSQI
     FSKFGITTTF VDPTDLDAWK NAVRPETKMF FLETPSNPLT EVADIEAIGK IAKASNALFV
     VDNCFCSPAL QQPLKLGADV VMHSATKFLD GQGRVLGGAL VGSKQFIMEK VFPFVRSAGP
     TLSAFNAWVL LKGMETLSLR VEKQSANALE IARWLETHPA VNRVFYPGLE SHPQHALAMR
     QQKAGGAILS FELKGDTPEQ MRANAWRVID NTKICSITGN LGDTRTTITH PATTTHGRVT
     SEARAAAGIS EGLIRLAVGL ENAGDIRGDL ERGLAG
//

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