LeishMANIAdb
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Putative NADH-dependent fumarate reductase

Quick info Annotations Function or PPIs Localization Phosphorylation Abundance Expansion Sequence features Structure Function Putative motif mimicry Homologs Download

Quick info

Protein:
Putative NADH-dependent fumarate reductase
Gene product:
NADH-dependent fumarate reductase - putative
Species:
Leishmania infantum
UniProt:
A4IB12_LEIIN
TriTrypDb:
LINF_350016600
Length:
1147

Annotations

Annotations by Jardim et al.

Tricarboxylic acid cycle, NADH-dependent fumarate reductase

Localization

Secreted promastigote
Source Evidence on protein Close homologs
Cuervo et al. no yes: 0
Hassani et al. no yes: 0
Forrest at al. (metacyclic) no yes: 0
Forrest at al. (procyclic) no yes: 0
Silverman et al. no yes: 0
Pissara et al. yes yes: 15
Secreted amastigote
Source Evidence on protein Close homologs
Pires et al. no yes: 0
Exosome
Source Evidence on protein Close homologs
Silverman et al. no yes: 0
Glycosome
Source Evidence on protein Close homologs
Jamdhade et al. no yes: 16
Predictions
Source Evidence on protein Close homologs
DeepLoc
SignalP6 no yes: 0, no: 19
NetGPI no yes: 0, no: 19
Cellular components
TermNameLevelCount
GO:0005737 cytoplasm 2 1
GO:0005777 peroxisome 6 1
GO:0005815 microtubule organizing center 2 1
GO:0020015 glycosome 7 1
GO:0036064 ciliary basal body 3 1
GO:0042579 microbody 5 1
GO:0043226 organelle 2 1
GO:0043227 membrane-bounded organelle 3 1
GO:0043229 intracellular organelle 3 1
GO:0043231 intracellular membrane-bounded organelle 4 1
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Phosphorylation

Promastigote/Amastigote: 9

Abundance

Amastigote (protein)
Source Evidence on protein Close homologs
Pescher et al. (upgregulation) no yes: 0
Promastigote and amastigote
Source Evidence on protein Close homologs
Lahav et al.
- mRNA
- Protein

Expansion

Sequence features

A4IB12
Sequence
MSA
Disorder
Secondary
Topology
Domains
SignalP
GPI
Phosphorylations
ELMs

Structure

Predicted structure by AlphaFold2

Related structures:

AlphaFold database: A4IB12

Function

Biological processes
TermNameLevelCount
GO:0006807 nitrogen compound metabolic process 2 20
GO:0008152 metabolic process 1 20
GO:0017013 protein flavinylation 5 20
GO:0019538 protein metabolic process 3 20
GO:0036211 protein modification process 4 20
GO:0043170 macromolecule metabolic process 3 20
GO:0043412 macromolecule modification 4 20
GO:0044238 primary metabolic process 2 20
GO:0071704 organic substance metabolic process 2 20
GO:1901564 organonitrogen compound metabolic process 3 20
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Molecular functions
TermNameLevelCount
GO:0000166 nucleotide binding 3 19
GO:0003824 catalytic activity 1 20
GO:0005488 binding 1 20
GO:0010181 FMN binding 4 19
GO:0016156 fumarate reductase (NADH) activity 5 1
GO:0016491 oxidoreductase activity 2 20
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors 3 1
GO:0016628 oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor 4 1
GO:0016740 transferase activity 2 20
GO:0032553 ribonucleotide binding 3 19
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Putative motif mimicry

LeishmaniaFromToDomain/MotifScore
CLV_C14_Caspase3-7 511 515 PF00656 0.299
CLV_NRD_NRD_1 1006 1008 PF00675 0.337
CLV_NRD_NRD_1 182 184 PF00675 0.334
CLV_NRD_NRD_1 338 340 PF00675 0.400
CLV_NRD_NRD_1 502 504 PF00675 0.297
CLV_NRD_NRD_1 832 834 PF00675 0.364
CLV_NRD_NRD_1 992 994 PF00675 0.434
CLV_PCSK_FUR_1 378 382 PF00082 0.441
CLV_PCSK_KEX2_1 257 259 PF00082 0.259
CLV_PCSK_KEX2_1 338 340 PF00082 0.312
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Homologs

ProteinTaxonomySequence identityCoverage
A0A0N0P690 Leptomonas seymouri 80% 100%
A0A0N1I186 Leptomonas seymouri 59% 93%
A0A0S4IK89 Bodo saltans 55% 96%
A0A0S4IZL1 Bodo saltans 56% 96%
A0A1X0NJ99 Trypanosomatidae 60% 93%
A0A3Q8IJ78 Leishmania donovani 100% 100%
A0A3S5H7Y6 Leishmania donovani 59% 96%
A0A422NIA0 Trypanosoma rangeli 62% 89%
A4HMB4 Leishmania braziliensis 59% 100%
A4HMD9 Leishmania braziliensis 90% 100%
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LeishMANIAdb - Server version: v0.0.2. - Database version: v0.0.1. - ChangeLog - © 2022-2025 Protein Bioinformatics Research Group, Institute of Enzymology, RCNS