(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIV0_GEOS0

ID   A0A0F6BIV0_GEOS0        Unreviewed;       298 AA.
AC   A0A0F6BIV0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 36.
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=GY4MC1_0519 {ECO:0000313|EMBL:ADP73351.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73351.1};
RN   [1] {ECO:0000313|EMBL:ADP73351.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73351.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the radical-mediated insertion of two sulfur atoms
CC       into the C-6 and C-8 positions of the octanoyl moiety bound to the
CC       lipoyl domains of lipoate-dependent enzymes, thereby converting the
CC       octanoylated domains into lipoylated derivatives. {ECO:0000256|HAMAP-
CC       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 = (R)-
CC         N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S]
CC         cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-
CC         methionine + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16585,
CC         Rhea:RHEA-COMP:9928, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC         Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:14568, Rhea:RHEA-COMP:14569,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:29919, ChEBI:CHEBI:33722, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:78809, ChEBI:CHEBI:83100; EC=2.8.1.8;
CC         Evidence={ECO:0000256|HAMAP-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 coordinated
CC       with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {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]. {ECO:0000256|HAMAP-Rule:MF_00206}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206,
CC       ECO:0000256|SAAS:SAAS01101439}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00206}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002293; ADP73351.1; -; Genomic_DNA.
DR   RefSeq; WP_003248290.1; NC_014650.1.
DR   EnsemblBacteria; ADP73351; ADP73351; GY4MC1_0519.
DR   GeneID; 29236826; -.
DR   KEGG; gmc:GY4MC1_0519; -.
DR   KO; K03644; -.
DR   OMA; PYCDIDF; -.
DR   OrthoDB; 1184806at2; -.
DR   BioCyc; GSP581103:G1GOQ-570-MONOMER; -.
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; IPR031691; LIAS_N.
DR   InterPro; IPR003698; Lipoyl_synth.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR10949; PTHR10949; 1.
DR   Pfam; PF16881; LIAS_N; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF005963; Lipoyl_synth; 1.
DR   SFLD; SFLDF00271; lipoyl_synthase; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00510; lipA; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BIV0.
DR   SWISS-2DPAGE; A0A0F6BIV0.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206, ECO:0000256|SAAS:SAAS01101443};
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   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00206, ECO:0000313|EMBL:ADP73351.1}.
FT   DOMAIN          57..265
FT                   /note="Elp3"
FT                   /evidence="ECO:0000259|SMART:SM00729"
FT   METAL           40
FT                   /note="Iron-sulfur 1 (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT   METAL           45
FT                   /note="Iron-sulfur 1 (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT   METAL           51
FT                   /note="Iron-sulfur 1 (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT   METAL           67
FT                   /note="Iron-sulfur 2 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT   METAL           71
FT                   /note="Iron-sulfur 2 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT   METAL           74
FT                   /note="Iron-sulfur 2 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
SQ   SEQUENCE   298 AA;  33959 MW;  689F8BD1635F4900 CRC64;
     MATKEEHLRK PDWLKIKLNT NENYTGLKKL MRENRLHTVC EEAKCPNIHE CWAARRTATF
     MILGNVCTRA CRFCAVKTGL PTELDWQEPE RVAESVRLMN LKHVVVTAVA RDDLKDGGAA
     VFAETIRAIR RKNPFTTIEV LPSDMGGVYE NLKTLMDARP DILNHNIETV RRLTPRVRAR
     ATYERSLEFL RRAKELQPDI PTKSSIMVGL GETKEEIIEA MDDLRANHVD ILTIGQYLQP
     TKKHLKVVKY YHPDEFKELK EIALSKGFTH CEAGPLVRSS YHADEQVNAA SAARQAKA
//

If you have problems or comments...

PBIL Back to PBIL home page