(data stored in ACNUC7421 zone)

HOGENOM: FRATN_1_PE1006

ID   FRATN_1_PE1006                       STANDARD;      PRT;   327 AA.
AC   FRATN_1_PE1006; A0Q6Q2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Lipoyl synthase; EC=2.8.1 8;AltName: Full=Lip-syn;
DE   Short=LS;AltName: Full=Lipoate synthase;AltName: Full=Lipoic acid
DE   synthase;AltName: Full=Sulfur insertion protein lipA; (FRATN_1.PE1006).
GN   Name=lipA; OrderedLocusNames=FTN_1030;
OS   FRANCISELLA NOVICIDA U112.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=401614;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FRATN_1.PE1006.
CC       Francisella tularensis subsp. novicida U112, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:LIPA_FRATN
CC   -!- FUNCTION: Catalyzes the radical-mediated insertion of two sulfur
CC       atoms into the C-6 and C-8 positions of the octanoyl moiety bound
CC       to the lipoyl domains of lipoate-dependent enzymes, thereby
CC       converting the octanoylated domains into lipoylated derivatives
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-(octanoyl)lysine + 2 sulfur + 2
CC       S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 L-
CC       methionine + 2 5'-deoxyadenosine.
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters per subunit. One cluster is
CC       coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC       methionine (By similarity).
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl
CC       synthase family.
CC   -!- GENE_FAMILY: HOG000235998 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A0Q6Q2; -.
DR   EMBL; CP000439; ABK89917.1; -; Genomic_DNA.
DR   RefSeq; YP_898671.1; NC_008601.1.
DR   ProteinModelPortal; A0Q6Q2; -.
DR   STRING; A0Q6Q2; -.
DR   GeneID; 4547962; -.
DR   GenomeReviews; CP000439_GR; FTN_1030.
DR   KEGG; ftn:FTN_1030; -.
DR   eggNOG; COG0320; -.
DR   OMA; SWGLDYI; -.
DR   ProtClustDB; PRK05481; -.
DR   BioCyc; FTUL401614:FTN_1030-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016992; F:lipoate synthase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_00206; Lipoyl_synth; 1; -.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR003698; Lipoate_synth.
DR   InterPro; IPR007197; rSAM.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR10949; Lipoate_synth; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF005963; Lipoyl_synth; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00510; LipA; 1.
DR   HOGENOMDNA; FRATN_1.PE1006; -.
KW   lipoyl synthase;
KW   4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; S-adenosyl-L-methionine; Transferase.
SQ   SEQUENCE   327 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKEISGIKVK VESGSKYTTD HGFHAVKDGI RNKKENAVHV RKPDWLKVQK QDSKEYLKVK
     SITKKHKLST VCEEARCPNI NECWSHGTAT IMLMGSVCTR ACKFCSVDTG NPKGWLDKDE
     PMNAAESVKL MGLEYVVLTS VDRDDLEDGG AGHYAATITA IKNLDENIKV EALTPDFAGI
     NENIDKIINT KVDVIAQNIE TVERLTHPVR DPRAGYWQTL NFLKYVKQKS PNVLTKTSIM
     VGLGETDEEI YKTMDDARSV GVDIITLGQY MQPTKHHLSV ERFVTPQQFE EYRKVGLEKG
     FLEVASGPMV RSSYRADRVF KRNNLDL
//

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