Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q1GGW2

Entry ID Method Resolution Chain Position Source
AF-Q1GGW2-F1 Predicted AlphaFoldDB

No variants for Q1GGW2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q1GGW2

No associated diseases with Q1GGW2

3 regional properties for Q1GGW2

Type Name Position InterPro Accession
domain Elp3/MiaA/NifB-like, radical SAM core domain 71 - 279 IPR006638
domain Radical SAM 14 - 304 IPR007197
domain Lipoyl synthase, N-terminal 13 - 60 IPR031691

Functions

Description
EC Number 2.8.1.8 Sulfurtransferases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

3 GO annotations of molecular function

Name Definition
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
lipoate synthase activity Catalysis of the reaction: protein N6-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N6-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosyl.
metal ion binding Binding to a metal ion.

1 GO annotations of biological process

Name Definition
protein lipoylation The lipoylation of peptidyl-lysine to form peptidyl-N6-lipoyl-L-lysine.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRDLKIPEQR HPEKAHRPDN AQPKKPSWIR VKAPGGKGYA ETHKIMRENN LVTVCEEAGC
70 80 90 100 110 120
PNVGECWSQG HATMMIMGEI CTRGCTFCNI ATGRPDTLDA FEPGRVAHAV QKLGLNHVVI
130 140 150 160 170 180
TSVDRDDLED GGADHFAQTI RAVRHRSPQT TIEILTPDFL KCAPEVLETV VEAKPDVFNH
190 200 210 220 230 240
NLETVPGLYP EVRPGARYFH SLRLLQRVKE LDPSIFTKSG IMVGLGEQAP QVKQVMDDMR
250 260 270 280 290 300
AADVDFLTIG QYLQPTPKHH AVDRFVTPEE FESYEKAAYG KGFLMVSATP LTRSSYHAGD
310
DFAKLRAARN AKLGLA