LIPA2_THEVB
ID LIPA2_THEVB Reviewed; 290 AA.
AC Q8DLC2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Lipoyl synthase 2 {ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000303|PubMed:25100160};
DE EC=2.8.1.8 {ECO:0000255|HAMAP-Rule:MF_00206};
DE AltName: Full=Lip-syn 2 {ECO:0000255|HAMAP-Rule:MF_00206};
DE Short=LS 2 {ECO:0000255|HAMAP-Rule:MF_00206};
DE AltName: Full=Lipoate synthase 2 {ECO:0000255|HAMAP-Rule:MF_00206};
DE AltName: Full=Lipoic acid synthase 2 {ECO:0000255|HAMAP-Rule:MF_00206};
DE AltName: Full=Sulfur insertion protein LipA 2 {ECO:0000255|HAMAP-Rule:MF_00206};
GN Name=lipA2 {ECO:0000255|HAMAP-Rule:MF_00206, ECO:0000303|PubMed:25100160};
GN OrderedLocusNames=tll0574;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2] {ECO:0007744|PDB:4U0O, ECO:0007744|PDB:4U0P}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEXES WITH IRON-SULFUR
RP (4FE-4S) AND S-ADENOSYL-L-HOMOCYSTEINE, AND COFACTOR.
RX PubMed=25100160; DOI=10.1042/bj20140895;
RA Harmer J.E., Hiscox M.J., Dinis P.C., Fox S.J., Iliopoulos A., Hussey J.E.,
RA Sandy J., Van Beek F.T., Essex J.W., Roach P.L.;
RT "Structures of lipoyl synthase reveal a compact active site for controlling
RT sequential sulfur insertion reactions.";
RL Biochem. J. 464:123-133(2014).
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:0000255|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:0000255|HAMAP-Rule:MF_00206};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00206,
CC ECO:0000269|PubMed:25100160};
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:0000255|HAMAP-Rule:MF_00206, ECO:0000269|PubMed:25100160};
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:0000255|HAMAP-Rule:MF_00206}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00206}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase
CC family. {ECO:0000255|HAMAP-Rule:MF_00206}.
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DR EMBL; BA000039; BAC08126.1; -; Genomic_DNA.
DR RefSeq; NP_681364.1; NC_004113.1.
DR RefSeq; WP_011056422.1; NC_004113.1.
DR PDB; 4U0O; X-ray; 1.60 A; B=1-290.
DR PDB; 4U0P; X-ray; 1.62 A; B=1-290.
DR PDBsum; 4U0O; -.
DR PDBsum; 4U0P; -.
DR AlphaFoldDB; Q8DLC2; -.
DR SMR; Q8DLC2; -.
DR STRING; 197221.22294295; -.
DR EnsemblBacteria; BAC08126; BAC08126; BAC08126.
DR KEGG; tel:tll0574; -.
DR PATRIC; fig|197221.4.peg.606; -.
DR eggNOG; COG0320; Bacteria.
DR OMA; GRCPNRG; -.
DR OrthoDB; 1184806at2; -.
DR UniPathway; UPA00538; UER00593.
DR Proteomes; UP000000440; 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:0102552; F:lipoyl synthase activity (acting on glycine-cleavage complex H protein; IEA:UniProtKB-EC.
DR GO; GO:0102553; F:lipoyl synthase activity (acting on pyruvate dehydrogenase E2 protein); IEA:UniProtKB-EC.
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.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..290
FT /note="Lipoyl synthase 2"
FT /id="PRO_0000102367"
FT DOMAIN 49..272
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 37
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00206,
FT ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O,
FT ECO:0007744|PDB:4U0P"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00206,
FT ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O,
FT ECO:0007744|PDB:4U0P"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00206,
FT ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O,
FT ECO:0007744|PDB:4U0P"
FT BINDING 63
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:0000255|HAMAP-Rule:MF_00206,
FT ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O,
FT ECO:0007744|PDB:4U0P"
FT BINDING 67
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:0000255|HAMAP-Rule:MF_00206,
FT ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O,
FT ECO:0007744|PDB:4U0P"
FT BINDING 70
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:0000255|HAMAP-Rule:MF_00206,
FT ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O,
FT ECO:0007744|PDB:4U0P"
FT BINDING 283
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00206,
FT ECO:0000269|PubMed:25100160, ECO:0007744|PDB:4U0O"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:4U0P"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:4U0O"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:4U0O"
FT TURN 43..48
FT /evidence="ECO:0007829|PDB:4U0O"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:4U0O"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:4U0O"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:4U0P"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4U0P"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:4U0O"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:4U0O"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:4U0O"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:4U0O"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:4U0O"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:4U0O"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:4U0O"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4U0O"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:4U0O"
FT HELIX 186..199
FT /evidence="ECO:0007829|PDB:4U0O"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:4U0O"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:4U0O"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:4U0O"
FT HELIX 256..269
FT /evidence="ECO:0007829|PDB:4U0O"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:4U0O"
FT TURN 282..287
FT /evidence="ECO:0007829|PDB:4U0O"
SQ SEQUENCE 290 AA; 31735 MW; 60BE127E2B9A59D9 CRC64;
MALSRPLPSW LRKPLGKASE ISTVQRLVRQ YGIHTICEEG RCPNRGECYG QKTATFLLLG
PTCTRACAFC QVEKGHAPAA VDPEEPTKIA AAVATLGLRY VVLTSVARDD LPDQGAGQFV
ATMAAIRQRC PGTEIEVLSP DFRMDRGRLS QRDCIAQIVA AQPACYNHNL ETVRRLQGPV
RRGATYESSL RVLATVKELN PDIPTKSGLM LGLGETEAEI IETLKDLRRV GCDRLTLGQY
LPPSLSHLPV VKYWTPEEFN TLGNIARELG FSHVRSGPLV RSSYHAAEGG
