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 Q5BIP7

Entry ID Method Resolution Chain Position Source
AF-Q5BIP7-F1 Predicted AlphaFoldDB

33 variants for Q5BIP7

Variant ID(s) Position Change Description Diseaes Association Provenance
rs452181238 16 V>E No EVA
rs472376478 21 V>G No EVA
rs440871499 50 S>C No EVA
rs464009156 67 K>T No EVA
rs470544468 84 I>M No EVA
rs453491864 92 K>E No EVA
rs453491864 92 K>Q No EVA
rs442231426 94 K>E No EVA
rs462347178 98 R>W No EVA
rs475736480 100 L>V No EVA
rs449130731 118 W>C No EVA
rs134264166 126 A>P No EVA
rs135655447 127 T>P No EVA
rs480356498 142 R>G No EVA
rs211447555 158 N>S No EVA
rs1116041948 167 I>V No EVA
rs43463545 179 S>F No EVA
rs445459687 188 G>* No EVA
rs453892884 206 K>N No EVA
rs467421549 227 A>G No EVA
rs436188669 232 D>N No EVA
rs456156484 240 T>K No EVA
rs383164309 242 P>Q No EVA
rs476163485 243 E>* No EVA
rs481803679 247 K>T No EVA
rs723120812 279 M>I No EVA
rs442097144 297 R>C No EVA
rs1114511767 303 C>Y No EVA
rs455641313 307 G>* No EVA
rs444428383 312 P>T No EVA
rs467788859 362 N>H No EVA
rs436416145 365 A>V No EVA
rs469350283 366 K>* No EVA

No associated diseases with Q5BIP7

3 regional properties for Q5BIP7

Type Name Position InterPro Accession
domain Elp3/MiaA/NifB-like, radical SAM core domain 127 - 333 IPR006638
domain Radical SAM 67 - 362 IPR007197
domain Lipoyl synthase, N-terminal 4 - 111 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
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
Q5XIH4 Lias Lipoyl synthase, mitochondrial Rattus norvegicus (Rat) 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
MSLRCGGAVR TVGPRVFGRY VFSPVREVSF LPDEKKEFLQ SGPDLQEFIS GNLADKSTWD
70 80 90 100 110 120
EYKGNLKRQK GERLRLPPWL KTEIPMGKNY NKLKNTLRNL NLHTVCEEAR CPNIGECWGG
130 140 150 160 170 180
GEYATATATI MLMGDTCTRG CRFCSVKTAR NPPPLDANEP YNTAKAIAEW GLDYVVLTSV
190 200 210 220 230 240
DRDDMPDGGA EHFAKTVSYL KERNPKILVE CLTPDFRGDL KAIEKVALSG LDVYAHNVET
250 260 270 280 290 300
VPELQRKVRD PRANFDQSLR VLKHAKEVRP DVISKTSIML GLGENDEQVY ATMKALREAD
310 320 330 340 350 360
VDCLTLGQYM QPTKRHLKVE EYITPEKFKY WEKVGNELGF HYTASGPLVR SSYKAGEFFL
370
KNLVAKRKTK AL