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Protein

Acyl-[acyl-carrier-protein] dehydrogenase MbtN

Gene

mbtN

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dehydrogenation at the alpha-beta position of ACP-bound acyl chains. This results in the introduction of a double bond in the lipidic chain, which is further transferred to the epsilon-amino group of lysine residue in the mycobactin core by MbtK.1 Publication

Cofactori

FAD1 Publication

Pathwayi: mycobactin biosynthesis

This protein is involved in the pathway mycobactin biosynthesis, which is part of Siderophore biosynthesis.
View all proteins of this organism that are known to be involved in the pathway mycobactin biosynthesis and in Siderophore biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

UniPathwayiUPA00011.

Chemistry

SwissLipidsiSLP:000001256.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-[acyl-carrier-protein] dehydrogenase MbtN (EC:1.3.99.-)
Short name:
Acyl-ACP dehydrogenase MbtN
Alternative name(s):
Mycobactin synthase protein N
Gene namesi
Name:mbtN
Synonyms:fadE14
Ordered Locus Names:Rv1346
ORF Names:MTCY02B10.10
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1346.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386Acyl-[acyl-carrier-protein] dehydrogenase MbtNPRO_0000000538Add
BLAST

Proteomic databases

PaxDbiP9WQF9.

Expressioni

Inductioni

Induced by iron starvation conditions. Transcriptionally repressed by IdeR and iron.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv1346.

Structurei

Secondary structure

1
386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1712Combined sources
Helixi20 – 3213Combined sources
Helixi37 – 459Combined sources
Helixi48 – 536Combined sources
Helixi61 – 7313Combined sources
Helixi77 – 9620Combined sources
Helixi100 – 11011Combined sources
Beta strandi116 – 1194Combined sources
Helixi129 – 1313Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi142 – 15312Combined sources
Turni154 – 1574Combined sources
Beta strandi159 – 1679Combined sources
Beta strandi179 – 1857Combined sources
Helixi186 – 1883Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi197 – 1993Combined sources
Beta strandi205 – 21511Combined sources
Helixi216 – 2183Combined sources
Beta strandi219 – 2213Combined sources
Turni223 – 2253Combined sources
Helixi226 – 26237Combined sources
Helixi270 – 2723Combined sources
Helixi274 – 29926Combined sources
Helixi305 – 32925Combined sources
Helixi331 – 3344Combined sources
Turni337 – 3393Combined sources
Helixi342 – 3498Combined sources
Helixi350 – 3534Combined sources
Turni354 – 3563Combined sources
Helixi359 – 36810Combined sources
Helixi374 – 3807Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XVXX-ray2.30A/B2-386[»]
ProteinModelPortaliP9WQF9.
SMRiP9WQF9. Positions 5-381.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Phylogenomic databases

eggNOGiENOG4107Q3C. Bacteria.
ENOG410Y5AK. LUCA.
KOiK00257.
OMAiMSECMHI.
PhylomeDBiP9WQF9.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
InterProiIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.

Sequencei

Sequence statusi: Complete.

P9WQF9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAGSDLDDF RGLLAKAFDE RVVAWTAEAE AQERFPRQLI EHLGVCGVFD
60 70 80 90 100
AKWATDARPD VGKLVELAFA LGQLASAGIG VGVSLHDSAI AILRRFGKSD
110 120 130 140 150
YLRDICDQAI RGAAVLCIGA SEESGGSDLQ IVETEIRSRD GGFEVRGVKK
160 170 180 190 200
FVSLSPIADH IMVVARSVDH DPTSRHGNVA VVAVPAAQVS VQTPYRKVGA
210 220 230 240 250
GPLDTAAVCI DTWVPADALV ARAGTGLAAI SWGLAHERMS IAGQIAASCQ
260 270 280 290 300
RAIGITLARM MSRRQFGQTL FEHQALRLRM ADLQARVDLL RYALHGIAEQ
310 320 330 340 350
GRLELRTAAA VKVTAARLGE EVISECMHIF GGAGYLVDET TLGKWWRDMK
360 370 380
LARVGGGTDE VLWELVAAGM TPDHDGYAAV VGASKA
Length:386
Mass (Da):41,180
Last modified:April 16, 2014 - v1
Checksum:i60A2765380F89EFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44104.1.
PIRiA70740.
RefSeqiNP_215862.1. NC_000962.3.
WP_003406953.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP44104; CCP44104; Rv1346.
GeneIDi886844.
KEGGimtu:Rv1346.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44104.1.
PIRiA70740.
RefSeqiNP_215862.1. NC_000962.3.
WP_003406953.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XVXX-ray2.30A/B2-386[»]
ProteinModelPortaliP9WQF9.
SMRiP9WQF9. Positions 5-381.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1346.

Chemistry

SwissLipidsiSLP:000001256.

Proteomic databases

PaxDbiP9WQF9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44104; CCP44104; Rv1346.
GeneIDi886844.
KEGGimtu:Rv1346.

Organism-specific databases

TubercuListiRv1346.

Phylogenomic databases

eggNOGiENOG4107Q3C. Bacteria.
ENOG410Y5AK. LUCA.
KOiK00257.
OMAiMSECMHI.
PhylomeDBiP9WQF9.

Enzyme and pathway databases

UniPathwayiUPA00011.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
InterProiIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "IdeR, an essential gene in Mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response."
    Rodriguez G.M., Voskuil M.I., Gold B., Schoolnik G.K., Smith I.
    Infect. Immun. 70:3371-3381(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: ATCC 25618 / H37Rv.
  3. "A genetic locus required for iron acquisition in Mycobacterium tuberculosis."
    Krithika R., Marathe U., Saxena P., Ansari M.Z., Mohanty D., Gokhale R.S.
    Proc. Natl. Acad. Sci. U.S.A. 103:2069-2074(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ROLE IN MYCOBACTIN BIOSYNTHESIS, COFACTOR.
    Strain: ATCC 25618 / H37Rv.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.

Entry informationi

Entry nameiMBTN_MYCTU
AccessioniPrimary (citable) accession number: P9WQF9
Secondary accession number(s): L0T946, P63431, Q11016
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: December 9, 2015
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.