(data stored in ACNUC7421 zone)

SWISSPROT: A4ATD5_MARSH

ID   A4ATD5_MARSH            Unreviewed;       288 AA.
AC   A4ATD5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 84.
DE   RecName: Full=Lipoyl synthase {ECO:0000256|HAMAP-Rule:MF_00206};
DE            EC=2.8.1.8 {ECO:0000256|HAMAP-Rule:MF_00206};
DE   AltName: Full=Lip-syn {ECO:0000256|HAMAP-Rule:MF_00206};
DE            Short=LS {ECO:0000256|HAMAP-Rule:MF_00206};
DE   AltName: Full=Lipoate synthase {ECO:0000256|HAMAP-Rule:MF_00206};
DE   AltName: Full=Lipoic acid synthase {ECO:0000256|HAMAP-Rule:MF_00206};
DE   AltName: Full=Sulfur insertion protein LipA {ECO:0000256|HAMAP-Rule:MF_00206};
GN   Name=lipA {ECO:0000256|HAMAP-Rule:MF_00206};
GN   OrderedLocusNames=FB2170_16511 {ECO:0000313|EMBL:EAR00705.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00705.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00705.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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       {ECO:0000256|HAMAP-Rule:MF_00206}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[[Fe-S] cluster scaffold protein carrying a second [4Fe-
CC         4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2
CC         oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine =
CC         (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine +
CC         [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen
CC         sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:16585, Rhea:RHEA-COMP:9928, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:14568, Rhea:RHEA-COMP:14569, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17319, ChEBI:CHEBI:29034, ChEBI:CHEBI:29919,
CC         ChEBI:CHEBI:33722, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:78809,
CC         ChEBI:CHEBI:83100; EC=2.8.1.8; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00206};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00206};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. One cluster is
CC       coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC       methionine. {ECO:0000256|HAMAP-Rule:MF_00206};
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00206,
CC       ECO:0000256|SAAS:SAAS01179528}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl
CC       synthase family. {ECO:0000256|HAMAP-Rule:MF_00206}.
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DR   EMBL; CP002157; EAR00705.1; -; Genomic_DNA.
DR   RefSeq; WP_013304508.1; NC_014472.1.
DR   STRING; 313603.FB2170_16511; -.
DR   EnsemblBacteria; EAR00705; EAR00705; FB2170_16511.
DR   KEGG; fbc:FB2170_16511; -.
DR   eggNOG; ENOG4105C0G; Bacteria.
DR   eggNOG; COG0320; LUCA.
DR   HOGENOM; HOG000235998; -.
DR   KO; K03644; -.
DR   OMA; PYCDIDF; -.
DR   OrthoDB; 1184806at2; -.
DR   BioCyc; MSP313603:G1GNS-80-MONOMER; -.
DR   UniPathway; UPA00538; UER00593.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016992; F:lipoate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00206; Lipoyl_synth; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR003698; Lipoyl_synth.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR10949; PTHR10949; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF005963; Lipoyl_synth; 1.
DR   SFLD; SFLDF00271; lipoyl_synthase; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00510; lipA; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4ATD5.
DR   SWISS-2DPAGE; A4ATD5.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   DOMAIN       58    264       Elp3. {ECO:0000259|SMART:SM00729}.
FT   COILED      210    230       {ECO:0000256|SAM:Coils}.
FT   METAL        42     42       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL        47     47       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL        53     53       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL        68     68       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL        72     72       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   METAL        75     75       Iron-sulfur 2 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_00206}.
SQ   SEQUENCE   288 AA;  32564 MW;  DA5270D09E9C56A0 CRC64;
     MGVDSVAPPK GKPKWLRVKL PTGKKYTQLR GLVDKYDLHT ICTSGSCPNM GECWGEGTAT
     FMILGNICTR SCGFCGVKTG RPEDVDWAEP EKVARSINLM GIKHAVITSV DRDDLKDMGS
     IIWAETVKAI RRMNPSTTLE TLIPDFQGIE KHLDRIIEVR PEVVSHNMET VKRLTREVRI
     QAKYERSLEA LRYLRDNGAN RTKSGIMLGL GELEEEVLET MEDLRKARVD VVTIGQYLQP
     SKKHLPVKEF ILPEQFKKYE EAGLKMGFRH VESGALVRSS YKAHKHIN
//

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