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 Q16W22

Entry ID Method Resolution Chain Position Source
AF-Q16W22-F1 Predicted AlphaFoldDB

No variants for Q16W22

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q16W22

No associated diseases with Q16W22

3 regional properties for Q16W22

Type Name Position InterPro Accession
domain Elp3/MiaA/NifB-like, radical SAM core domain 132 - 341 IPR006638
domain Radical SAM 70 - 366 IPR007197
domain Lipoyl synthase, N-terminal 23 - 116 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.

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
MSQISSNLLR NTVQNGKFGC LKNSIQCKHT AANPLEKIRE RLESGPSFQD FVQNPSYNRD
70 80 90 100 110 120
DWTDYEGKLR REKGENDRLR LPPWLKTKIP MGKNFSRIKD QLRELKLATV CEEAKCPNIG
130 140 150 160 170 180
ECWGGGEHGT QTATIMLMGD TCTRGCRFCS VKTARVPPPL DPAEPTNTAS AIASWGLDYI
190 200 210 220 230 240
VLTSVDRDDL PDGGSNHIAA TIREIKRQNP RIFVECLAPD FRGDLECVKV VAQSGLDVYA
250 260 270 280 290 300
HNIETVEALT PFVRDRRARY RQSLDVLRSI KEINPSMITK TSIMLGLGET DEQIEQTMKD
310 320 330 340 350 360
LRSVGVDCLT LGQYMQPTKR HLKVIEYVTP EKFKHWETRG NELGFLYTAS GPLVRSSYKA
370 380 390
GEFFITSILK NRAEEAERRK EAAGGQDTKT EQT