(data stored in SCRATCH zone)

SWISSPROT: C6AZH5_RHILS

ID   C6AZH5_RHILS            Unreviewed;       394 AA.
AC   C6AZH5;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 55.
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=Rleg_0190 {ECO:0000313|EMBL:ACS54501.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54501.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54501.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54501.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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: O(4)-succinyl-L-homoserine + H(2)S = L-
CC       homocysteine + succinate. {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; CP001622; ACS54501.1; -; Genomic_DNA.
DR   RefSeq; WP_012755917.1; NC_012850.1.
DR   ProteinModelPortal; C6AZH5; -.
DR   EnsemblBacteria; ACS54501; ACS54501; Rleg_0190.
DR   KEGG; rlg:Rleg_0190; -.
DR   HOGENOM; HOG000246417; -.
DR   KO; K10764; -.
DR   OMA; AVDNCFC; -.
DR   OrthoDB; POG091H053G; -.
DR   BioCyc; RLEG395491:GHX2-192-MONOMER; -.
DR   UniPathway; UPA00051; UER00449.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProtKB-HAMAP.
DR   GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-HAMAP.
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; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR11808; PTHR11808; 1.
DR   PANTHER; PTHR11808:SF71; PTHR11808:SF71; 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.
PE   3: Inferred from homology;
DR   PRODOM; C6AZH5.
DR   SWISS-2DPAGE; C6AZH5.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Lyase {ECO:0000313|EMBL:ACS54501.1};
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   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   394 AA;  42701 MW;  8C93C151854803B1 CRC64;
     MSKTWRPATQ LVHGGTLRSQ YGETSEAIYL TQGFVYETSE AAEARFKGET EGFIYARYGS
     PTNDMFEKRM CMLEGAEDAR ATASGMAAVT AAILCQLKSG DHIVAARALF GSCRWVVETL
     APKYGIDCTL IDGRDLANWE KAITPKTKVF FLESPTNPTL EVIDIAGVAK LANQVGAKVV
     VDNVFATPLF QKPLELGAHI VVYSATKHID GQGRCLGGVV LSDKEWIDEN LHDYFRHTGP
     AMSPFNAWTL LKGIETLPLR VRQQTENAAK IADFLAEQGK VAKVIYPGRK DHPQADIIAK
     QMTGGSTLVA FELKGGKDAA FALQNALDIV KISNNLGDSK SLITHPATTT HKNLTDEARA
     ELGISPGTVR LSAGIEDTDD LIEDFAKALD KVLA
//

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