(data stored in SCRATCH zone)

SWISSPROT: B1K360_BURCC

ID   B1K360_BURCC            Unreviewed;       396 AA.
AC   B1K360;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 60.
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   OrderedLocusNames=Bcenmc03_3562 {ECO:0000313|EMBL:ACA92714.1};
OS   Burkholderia cenocepacia (strain MC0-3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA92714.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT   3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000959; ACA92714.1; -; Genomic_DNA.
DR   RefSeq; WP_011694679.1; NC_010515.1.
DR   EnsemblBacteria; ACA92714; ACA92714; Bcenmc03_3562.
DR   KEGG; bcm:Bcenmc03_3562; -.
DR   HOGENOM; HOG000246417; -.
DR   KO; K10764; -.
DR   OMA; AVDNCFC; -.
DR   BioCyc; BCEN406425:G1GBC-3783-MONOMER; -.
DR   UniPathway; UPA00051; UER00449.
DR   Proteomes; UP000002169; Chromosome 2.
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; B1K360.
DR   SWISS-2DPAGE; B1K360.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002169};
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   Transferase {ECO:0000256|HAMAP-Rule:MF_02056,
KW   ECO:0000313|EMBL:ACA92714.1}.
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;  42613 MW;  72F5FE97C5A669BB CRC64;
     MDDSLNFDTL AVRAGTLRSD FNEHSEALFL TSSFCFSSAA DAAERFANSE DYFTYSRFTN
     PTVTMFQERL AALEGGEACI ATASGMAAIM SVVMSALQAG DHLVSSRSLF GSTLGMFSQI
     FSKFGITTTF VDPTDLNAWQ EAVRPETKMF FLETPSNPLT ELADIEAIGK IAKAANALFV
     VDNCFCSPVL QQPLKLGADV VMHSATKFLD GQGRVLGGAL VGSKEFIMGK VFPFVRSAGP
     TLSAFNAWVL LKGMETLSLR VEKQSANALE IARWLDSHPA VARVFYPGLE SHPQHELAKR
     QQKAGGAIVS FELKGDTPEQ QRANAWRVID GTKLVSITGN LGDTRTTITH PATTTHGRIT
     PEARAAAGIT EGLIRLAVGL EHAGDIRNDL ARGLDG
//

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