GenomeNet

Database: UniProt
Entry: A0A1Q2M9M9_9GAMM
LinkDB: A0A1Q2M9M9_9GAMM
Original site: A0A1Q2M9M9_9GAMM 
ID   A0A1Q2M9M9_9GAMM        Unreviewed;       344 AA.
AC   A0A1Q2M9M9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   ORFNames=Mag101_04750 {ECO:0000313|EMBL:AQQ69384.1};
OS   Microbulbifer agarilyticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Microbulbiferaceae; Microbulbifer.
OX   NCBI_TaxID=260552 {ECO:0000313|EMBL:AQQ69384.1, ECO:0000313|Proteomes:UP000188219};
RN   [1] {ECO:0000313|EMBL:AQQ69384.1, ECO:0000313|Proteomes:UP000188219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GP101 {ECO:0000313|EMBL:AQQ69384.1,
RC   ECO:0000313|Proteomes:UP000188219};
RA   Jung J., Bae S.S., Baek K.;
RT   "Genome of Microbulbifer agarilyticus GP101.";
RL   Submitted (FEB-2017) 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 = 2 5'-
CC         deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2
CC         hydrogen sulfide + 2 L-methionine + N(6)-[(R)-dihydrolipoyl]-L-lysyl-
CC         [protein] + 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|ARBA:ARBA00001264, 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 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]: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00206}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206}.
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; CP019650; AQQ69384.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2M9M9; -.
DR   STRING; 260552.Mag101_04750; -.
DR   KEGG; maga:Mag101_04750; -.
DR   eggNOG; COG0320; Bacteria.
DR   OrthoDB; 9787898at2; -.
DR   UniPathway; UPA00538; UER00593.
DR   Proteomes; UP000188219; 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   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00206; Lipoyl_synth; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR031691; LIAS_N.
DR   InterPro; IPR003698; Lipoyl_synth.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR00510; lipA; 1.
DR   PANTHER; PTHR10949; LIPOYL SYNTHASE; 1.
DR   PANTHER; PTHR10949:SF0; LIPOYL SYNTHASE, MITOCHONDRIAL; 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; SFLDG01058; lipoyl_synthase_like; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00206};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00206};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_00206};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00206}; Reference proteome {ECO:0000313|Proteomes:UP000188219};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_00206}; Transferase {ECO:0000256|HAMAP-Rule:MF_00206}.
FT   DOMAIN          103..320
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   BINDING         91
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT   BINDING         96
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT   BINDING         102
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT   BINDING         117
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT   BINDING         121
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT   BINDING         124
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
FT   BINDING         331
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00206"
SQ   SEQUENCE   344 AA;  38879 MW;  4C61ED11DE78DE2B CRC64;
     MKATEVTPAE VNPSETAKPD LVPVKRTRRL QQGEKLRDGE KVERIPVKVI ASDQTLRKPD
     WIRVKVPSVK ASKEVERIKS ILRSQKLATV CEEASCPNLG ECFSGGTATF MIMGEICTRR
     CPFCDVGHGK PNPLDPDEPQ QLAEAIAAMS LRYVVITSVD RDDLRDGGAE HFAECIKQSR
     ALSPNLQVEI LTPDFRGRMD VALDILEAEA PDVFNHNLET VPRLYRESRP GANYKWSLKL
     LQEYKKRRPD VLTKSGLMVG LGETKEEIFE VLDDMRAHDI DMLTIGQYLQ PSKEHLPVQR
     YVHPDEFEEY RVYAEKIGFK HAACGPMVRS SYHADKQAHG EEVK
//
DBGET integrated database retrieval system