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 B9I666

Entry ID Method Resolution Chain Position Source
AF-B9I666-F1 Predicted AlphaFoldDB

No variants for B9I666

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B9I666

No associated diseases with B9I666

3 regional properties for B9I666

Type Name Position InterPro Accession
domain Elp3/MiaA/NifB-like, radical SAM core domain 128 - 337 IPR006638
domain Radical SAM 71 - 364 IPR007197
domain Lipoyl synthase, N-terminal 74 - 112 IPR031691

Functions

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

2 GO annotations of cellular component

Name Definition
chloroplast A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
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.

2 GO annotations of biological process

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

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
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
MIEQSLSKPS FSLSIPIPQP PKSKSSFLCS YSKIRCESVD YPSSSKIDAK HPQISSINSN
70 80 90 100 110 120
GGGKMGSYTG RDPNVKKPEW LRQKAPQGER YDEVKESLSR LKLNTVCQEA QCPNIGECWN
130 140 150 160 170 180
GGGDGIATAT IMVLGDTCTR GCRFCAVKTS RNPPPPDPME PLNTALAIAS WGVDYIVITS
190 200 210 220 230 240
VDRDDLPDGG SGHFAQTVRA MKELKPEIMV ECLTSDFRGD LKAVDTLVHS GLDVFAHNVE
250 260 270 280 290 300
TVKRLQRIVR DPRAGYEQSL SVLKHAKISK KGMITKTSIM LGLGESDNEV KEAMADLRAI
310 320 330 340 350 360
GVDILTFGQY LQPTPLHLTV KEYVTPEKFA FWKEYGESIG FRYVASGPLV RSSYRAGELF
370
VKTMVKESVK EAAAIS