(data stored in ACNUC7421 zone)

SWISSPROT: C3MFC1_SINFN

ID   C3MFC1_SINFN            Unreviewed;       394 AA.
AC   C3MFC1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 51.
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   ECO:0000313|EMBL:ACP23958.1};
GN   OrderedLocusNames=NGR_c01560 {ECO:0000313|EMBL:ACP23958.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23958.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23958.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP23958.1; -; Genomic_DNA.
DR   RefSeq; WP_012706743.1; NC_012587.1.
DR   RefSeq; YP_002824711.1; NC_012587.1.
DR   STRING; 394.NGR_c01560; -.
DR   EnsemblBacteria; ACP23958; ACP23958; NGR_c01560.
DR   GeneID; 7790735; -.
DR   KEGG; rhi:NGR_c01560; -.
DR   PATRIC; fig|394.7.peg.2952; -.
DR   eggNOG; ENOG4105C28; Bacteria.
DR   eggNOG; COG0626; LUCA.
DR   HOGENOM; HOG000246417; -.
DR   KO; K10764; -.
DR   OMA; AVDNCFC; -.
DR   OrthoDB; POG091H053G; -.
DR   UniPathway; UPA00051; UER00449.
DR   Proteomes; UP000001054; Chromosome.
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; C3MFC1.
DR   SWISS-2DPAGE; C3MFC1.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02056};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
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:UP000001054};
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;  42770 MW;  EE20B7A2116FECEC CRC64;
     MSKTWRPATQ LVHGGTIRSQ YGETSEAIFL TQGFVYDSSE AAEARFKGET EGYIYARYGS
     PTNDMFEKRM CMLEGAEDAR ATASGMAAVS AAILCQVKAG DHIVAARALF GSCRWVVETL
     APKYGVECTL VDGRDLKNWE DAVRPNTKVF FLESPTNPTL EVIDIAGVAK LANQIGAKVV
     VDNVFATPLF QKPLELGAHI VVYSATKHID GQGRCLGGVV LSDKQWIDEN LHDYFRHTGP
     AMSPFNAWTL LKGIETLPLR VKQQTENARR VADFLAEQPQ VARVIYPGRK DHPQAGIIAK
     QMSGGSTLVA CELKGGKDAA FALQNALHIV RISNNLGDSK SLITHPATTT HKNLSDEART
     ELGISAGTVR FSAGIEDSDD LIEDFAKALT SVRA
//

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