(data stored in SCRATCH zone)

SWISSPROT: A0KFU6_AERHH

ID   A0KFU6_AERHH            Unreviewed;       387 AA.
AC   A0KFU6;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   13-FEB-2019, entry version 68.
DE   SubName: Full=O-succinylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:ABK39105.1};
DE            EC=2.5.1.48 {ECO:0000313|EMBL:ABK39105.1};
GN   Name=metB {ECO:0000313|EMBL:ABK39105.1};
GN   OrderedLocusNames=AHA_0589 {ECO:0000313|EMBL:ABK39105.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39105.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK39105.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; CP000462; ABK39105.1; -; Genomic_DNA.
DR   RefSeq; WP_011704557.1; NC_008570.1.
DR   RefSeq; YP_855122.1; NC_008570.1.
DR   STRING; 380703.AHA_0589; -.
DR   EnsemblBacteria; ABK39105; ABK39105; AHA_0589.
DR   GeneID; 4489256; -.
DR   KEGG; aha:AHA_0589; -.
DR   PATRIC; fig|380703.7.peg.585; -.
DR   eggNOG; ENOG4105C28; Bacteria.
DR   eggNOG; COG0626; LUCA.
DR   HOGENOM; HOG000246415; -.
DR   KO; K01739; -.
DR   OMA; HPGRMTH; -.
DR   BioCyc; AHYD380703:G1G7B-590-MONOMER; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR011821; O_succ_thio_ly.
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; TIGR02080; O_succ_thio_ly; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0KFU6.
DR   SWISS-2DPAGE; A0KFU6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Lyase {ECO:0000313|EMBL:ABK39105.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001434-2,
KW   ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Transferase {ECO:0000313|EMBL:ABK39105.1}.
FT   MOD_RES     197    197       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR001434-2}.
SQ   SEQUENCE   387 AA;  40935 MW;  45B446D2C0E59D80 CRC64;
     MTHKATQAVR TGIETDQQHG AVVPPIYLSS NYTFADFGEP RQYDYARSGN PTRTNLADAL
     AALEGGAGAV VTGTGMGAVH LVTTALLKAG DLLLAPHDCY GGTWRLFEYL AAKGHYRVQF
     VDQGDAAALA EALAQQPALV WVETPSNPLL RVVDIAAIAE ASHAAGAKVA VDNTFLSPLL
     QQPLALGADL VVHSTTKYIN GHSDVVGGVA IAKDPELADS LVWWANCLGL TSGAFDSYLT
     LRGLRTLAPR LRAHQENTDR ILAFLQQQPL VKRIYHPSLP SHPGHDIARR QQSGFGAMLS
     FELDCSEAGI RAFLAALTLF SVAESLGGVE SLVAHPASMT HRAMTPAAQQ AAGISSQLLR
     LSVGIEHGED LVADLAAAFA QAQQVAK
//

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