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 Q5XIH4

Entry ID Method Resolution Chain Position Source
AF-Q5XIH4-F1 Predicted AlphaFoldDB

No variants for Q5XIH4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5XIH4

No associated diseases with Q5XIH4

3 regional properties for Q5XIH4

Type Name Position InterPro Accession
domain Elp3/MiaA/NifB-like, radical SAM core domain 126 - 332 IPR006638
domain Radical SAM 121 - 340 IPR007197
domain Lipoyl synthase, N-terminal 4 - 110 IPR031691

Functions

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

1 GO annotations of cellular component

Name Definition
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

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.

6 GO annotations of biological process

Name Definition
inflammatory response The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages.
lipoate biosynthetic process The chemical reactions and pathways resulting in the formation of lipoate, 1,2-dithiolane-3-pentanoate, the anion derived from lipoic acid.
neural tube closure The last step in the formation of the neural tube, where the paired neural folds are brought together and fuse at the dorsal midline.
protein lipoylation The lipoylation of peptidyl-lysine to form peptidyl-N6-lipoyl-L-lysine.
response to lipopolysaccharide Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipopolysaccharide stimulus; lipopolysaccharide is a major component of the cell wall of gram-negative bacteria.
response to oxidative stress Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.

8 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5BIP7 LIAS Lipoyl synthase, mitochondrial Bos taurus (Bovine) PR
Q7JQW6 Las Lipoyl synthase, mitochondrial Drosophila melanogaster (Fruit fly) PR
O43766 LIAS Lipoyl synthase, mitochondrial Homo sapiens (Human) PR
B6TN12 LIP1P-1 Lipoyl synthase 1, chloroplastic Zea mays (Maize) PR
B9I666 LIP1P-1 Lipoyl synthase 1, chloroplastic Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) PR
B9N2B0 LIP1P-2 Lipoyl synthase 2, chloroplastic Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) PR
Q5ZAQ2 LIP1P-1 Lipoyl synthase 1, chloroplastic Oryza sativa subsp japonica (Rice) PR
Q8LEE8 LIP1P Lipoyl synthase, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MALRCWDAAR SLGSRIFGRY ACSVRALSSL PDEKKKFLHN GPDLQDFVSG DLADKSTWDD
70 80 90 100 110 120
YKGNLKRQKG ERLRLPPWLK TKIPMGKNYN KLKNTLRNLN LHTVCEEARC PNIGECWGGG
130 140 150 160 170 180
EYATATATIM LMGDTCTRGC RFCSVKTARN PPPLDPSEPD NTARAIAEWG LDYVVLTSVD
190 200 210 220 230 240
RDDVVDGGAE HIAKTVSCLK ERNPKILVEC LTPDFRGDLR AVEKVALSGL DVYAHNVETV
250 260 270 280 290 300
PELQRKVRDP RANFDQSLRV LKHAKEVQPD VVSKTSIMLG LGETDEQVYA TMKALRAADV
310 320 330 340 350 360
DCLTLGQYMQ PTKRHLKVEE YVTPEKFKYW EEVGNELGFH YTASGPLVRS SYKAGEFFLK
370
NLVAKRKTKV SKV