Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Long-chain-fatty-acid--CoA ligase FadD17

Gene

fadD17

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 activation of long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension.1 Publication

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

Pathway: fatty acid biosynthesis

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

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • long-chain fatty acid-CoA ligase activity Source: MTBBASE

GO - Biological processi

  • Actinobacterium-type cell wall biogenesis Source: UniProtKB
  • lipid biosynthetic process Source: UniProtKB
  • long-chain fatty acid biosynthetic process Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMTBRV:RV3506-MONOMER.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain-fatty-acid--CoA ligase FadD17 (EC:6.2.1.3)
Short name:
FACL
Alternative name(s):
Acyl-CoA synthetase
Gene namesi
Name:fadD17
Ordered Locus Names:Rv3506
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3506.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502Long-chain-fatty-acid--CoA ligase FadD17PRO_0000406787Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv3506.

Structurei

3D structure databases

ProteinModelPortaliO53551.
SMRiO53551. Positions 26-491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0318.
HOGENOMiHOG000052047.
KOiK00666.
OMAiPMFHGNA.
OrthoDBiEOG6VF30G.
PhylomeDBiO53551.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR030310. FadD17.
[Graphical view]
PANTHERiPTHR24096:SF115. PTHR24096:SF115. 1 hit.
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O53551-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPTHPTVTE LLLPLSEIDD RGVYFEDSFT SWRDHIRHGA AIAAALRERL
60 70 80 90 100
DPARPPHVGV LLQNTPFFSA TLVAGALSGI VPVGLNPVRR GAALAGDIAK
110 120 130 140 150
ADCQLVLTGS GSAEVPADVE HINVDSPEWT DEVAAHRDTE VRFRSADLAD
160 170 180 190 200
LFMLIFTSGT SGDPKAVKCS HRKVAIAGVT ITQRFSLGRD DVCYVSMPLF
210 220 230 240 250
HSNAVLVGWA VAAACQGSMA LRRKFSASQF LADVRRYGAT YANYVGKPLS
260 270 280 290 300
YVLATPELPD DADNPLRAVY GNEGVPGDID RFGRRFGCVV MDGFGSTEGG
310 320 330 340 350
VAITRTLDTP AGALGPLPGG IQIVDPDTGE PCPTGVVGEL VNTAGPGGFE
360 370 380 390 400
GYYNDEAAEA ERMAGGVYHS GDLAYRDDAG YAYFAGRLGD WMRVDGENLG
410 420 430 440 450
TAPIERVLMR YPDATEVAVY PVPDPVVGDQ VMAALVLAPG TKFDADKFRA
460 470 480 490 500
FLTEQPDLGH KQWPSYVRVS AGLPRTMTFK VIKRQLSAEG VACADPVWPI

RR
Length:502
Mass (Da):53,739
Last modified:June 1, 1998 - v1
Checksum:i0AF9A7B3B9C83A4D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46328.1.
PIRiD70806.
RefSeqiNP_218023.1. NC_000962.3.
WP_003901655.1. NZ_KK339370.1.
YP_006516995.1. NC_018143.2.

Genome annotation databases

EnsemblBacteriaiCCP46328; CCP46328; Rv3506.
GeneIDi888251.
KEGGimtu:Rv3506.
mtv:RVBD_3506.
PATRICi18156406. VBIMycTub87468_3913.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46328.1.
PIRiD70806.
RefSeqiNP_218023.1. NC_000962.3.
WP_003901655.1. NZ_KK339370.1.
YP_006516995.1. NC_018143.2.

3D structure databases

ProteinModelPortaliO53551.
SMRiO53551. Positions 26-491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3506.

Chemistry

ChEMBLiCHEMBL5783.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46328; CCP46328; Rv3506.
GeneIDi888251.
KEGGimtu:Rv3506.
mtv:RVBD_3506.
PATRICi18156406. VBIMycTub87468_3913.

Organism-specific databases

TubercuListiRv3506.

Phylogenomic databases

eggNOGiCOG0318.
HOGENOMiHOG000052047.
KOiK00666.
OMAiPMFHGNA.
OrthoDBiEOG6VF30G.
PhylomeDBiO53551.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciMTBRV:RV3506-MONOMER.

Miscellaneous databases

PROiO53551.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR030310. FadD17.
[Graphical view]
PANTHERiPTHR24096:SF115. PTHR24096:SF115. 1 hit.
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria."
    Trivedi O.A., Arora P., Sridharan V., Tickoo R., Mohanty D., Gokhale R.S.
    Nature 428:441-445(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ACYL-COA SYNTHETASE.
    Strain: ATCC 25618 / H37Rv.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.

Entry informationi

Entry nameiFAC17_MYCTU
AccessioniPrimary (citable) accession number: O53551
Secondary accession number(s): L0TCQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: June 1, 1998
Last modified: June 24, 2015
This is version 91 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.