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Protein

Acyl-[acyl-carrier-protein] dehydrogenase MbtN

Gene

mbtN

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: -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

  • siderophore biosynthetic process from catechol Source: MTBBASE

Keywordsi

Molecular functionOxidoreductase
LigandFAD, Flavoprotein

Enzyme and pathway databases

UniPathwayiUPA00011

Chemistry databases

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000005381 – 386Acyl-[acyl-carrier-protein] dehydrogenase MbtNAdd BLAST386

Proteomic databases

PaxDbiP9WQF9
PRIDEiP9WQF9

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

1386
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 17Combined sources12
Helixi20 – 32Combined sources13
Helixi37 – 45Combined sources9
Helixi48 – 53Combined sources6
Helixi61 – 73Combined sources13
Helixi77 – 96Combined sources20
Helixi100 – 110Combined sources11
Beta strandi116 – 119Combined sources4
Helixi129 – 131Combined sources3
Beta strandi135 – 139Combined sources5
Beta strandi142 – 153Combined sources12
Turni154 – 157Combined sources4
Beta strandi159 – 167Combined sources9
Beta strandi179 – 185Combined sources7
Helixi186 – 188Combined sources3
Beta strandi189 – 191Combined sources3
Beta strandi197 – 199Combined sources3
Beta strandi205 – 215Combined sources11
Helixi216 – 218Combined sources3
Beta strandi219 – 221Combined sources3
Turni223 – 225Combined sources3
Helixi226 – 262Combined sources37
Helixi270 – 272Combined sources3
Helixi274 – 299Combined sources26
Helixi305 – 329Combined sources25
Helixi331 – 334Combined sources4
Turni337 – 339Combined sources3
Helixi342 – 349Combined sources8
Helixi350 – 353Combined sources4
Turni354 – 356Combined sources3
Helixi359 – 368Combined sources10
Helixi374 – 380Combined sources7

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Phylogenomic databases

eggNOGiENOG4107Q3C Bacteria
ENOG410Y5AK LUCA
KOiK00257
OMAiRMMTRRQ
PhylomeDBiP9WQF9

Family and domain databases

Gene3Di1.10.540.10, 1 hit
InterProiView protein in InterPro
IPR006091 Acyl-CoA_Oxase/DH_cen-dom
IPR036250 AcylCo_DH-like_C
IPR009075 AcylCo_DH/oxidase_C
IPR013786 AcylCoA_DH/ox_N
IPR037069 AcylCoA_DH/ox_N_sf
IPR009100 AcylCoA_DH/oxidase_NM_dom
PfamiView protein in Pfam
PF00441 Acyl-CoA_dh_1, 1 hit
PF02770 Acyl-CoA_dh_M, 1 hit
PF02771 Acyl-CoA_dh_N, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiMBTN_MYCTU
AccessioniPrimary (citable) accession number: P9WQF9
Secondary accession number(s): L0T946, P63431, Q11016
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: May 23, 2018
This is version 26 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health