C3LM83

PR
Gene name
lplA
Protein name
Lipoate-protein ligase A
Names
Lipoate--protein ligase
Species
Vibrio cholerae serotype O1 (strain M66-2)
KEGG Pathway
vcm:VCM66_1343
EC number
6.3.1.20: Acid--ammonia (or amine) ligases (amide synthases)
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

28-105 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for C3LM83

Entry ID Method Resolution Chain Position Source
AF-C3LM83-F1 Predicted AlphaFoldDB

No variants for C3LM83

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C3LM83

No associated diseases with C3LM83

2 regional properties for C3LM83

Type Name Position InterPro Accession
domain Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain 29 - 216 IPR004143
domain Lipoate protein ligase, C-terminal 249 - 333 IPR019491

Functions

Description
EC Number 6.3.1.20 Acid--ammonia (or amine) ligases (amide synthases)
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.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
lipoate-protein ligase activity Catalysis of the lipoylation of a protein in two steps: ATP + (R)-lipoate + a -N6-(lipoyl)lysine + AMP + diphosphate (overall reaction): (1) ATP + (R)-lipoate = lipoyl-AMP + diphosphate; (2) lipoyl-AMP + a -N6-(lipoyl)lysine + AMP.

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
MTKTRILLSD STDPWFNLAV EDTIFRSMPA DQRVLFLWRN ADTVVIGRAQ NPWRECKTDR
70 80 90 100 110 120
MEQDKVKLAR RQTGGGAVFH DLGNTNFTFM AGKPEYDKEV STKIVLAGLQ KLGIHGVANG
130 140 150 160 170 180
RNDLVLEDEQ GIRKFSGSAY RETLDRGFHH GTLLLSADLN RLADYLNPDL KKLQAKGITS
190 200 210 220 230 240
VKSRVINLNT VKADIEHQQV CEAIMQAYCE HYQQQVEPEL ISPQSFFDLP GFEQKFAQQS
250 260 270 280 290 300
SWDWNFGQTP PFTHHMDERF SWGGVEVYLE VERGTIVQAT IFSDMLDPYP MEQLALRLSG
310 320 330
LTYNKTALEP CLAQLMQELP QYQLPLEEFQ RWFIDQID