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Protein

Long-chain-fatty-acid--AMP ligase FadD32

Gene

fadD32

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

Functioni

Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase (PKS) for further chain extension.1 Publication

Pathwayi: 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

  • adenylyltransferase activity Source: MTBBASE
  • ATP binding Source: UniProtKB-KW
  • ligase activity Source: UniProtKB

GO - Biological processi

  • Actinobacterium-type cell wall biogenesis Source: UniProtKB
  • fatty acid biosynthetic process Source: GO_Central
  • growth Source: MTBBASE
  • lipid biosynthetic process Source: UniProtKB
  • mycolate cell wall layer assembly 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

BioCyciMetaCyc:G185E-8097-MONOMER.
MTBH37RV:G185E-8097-MONOMER.
UniPathwayiUPA00094.

Chemistry databases

SwissLipidsiSLP:000000972.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain-fatty-acid--AMP ligase FadD32 (EC:6.2.1.-)
Short name:
FAAL
Alternative name(s):
Acyl-AMP synthetase
Gene namesi
Name:fadD32
Ordered Locus Names:Rv3801c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3801c.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi383F → A: Catalyzes the formation of acyl-CoA; when associated with A-481. 1 Publication1
Mutagenesisi481F → A: Catalyzes the formation of acyl-CoA; when associated with A-383. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004066341 – 637Long-chain-fatty-acid--AMP ligase FadD32Add BLAST637

Proteomic databases

PaxDbiO53580.

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv3801c.

Structurei

Secondary structure

1637
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 17Combined sources3
Helixi29 – 39Combined sources11
Turni40 – 42Combined sources3
Beta strandi43 – 50Combined sources8
Beta strandi58 – 63Combined sources6
Helixi64 – 81Combined sources18
Beta strandi87 – 90Combined sources4
Helixi96 – 108Combined sources13
Beta strandi110 – 114Combined sources5
Beta strandi120 – 122Combined sources3
Helixi124 – 134Combined sources11
Beta strandi137 – 141Combined sources5
Helixi143 – 154Combined sources12
Beta strandi163 – 166Combined sources4
Helixi167 – 169Combined sources3
Helixi172 – 177Combined sources6
Beta strandi187 – 194Combined sources8
Beta strandi197 – 200Combined sources4
Beta strandi202 – 207Combined sources6
Helixi210 – 222Combined sources13
Beta strandi229 – 232Combined sources4
Helixi239 – 249Combined sources11
Turni250 – 252Combined sources3
Beta strandi255 – 257Combined sources3
Helixi260 – 265Combined sources6
Helixi268 – 274Combined sources7
Beta strandi284 – 288Combined sources5
Helixi290 – 299Combined sources10
Beta strandi304 – 306Combined sources3
Beta strandi314 – 319Combined sources6
Helixi326 – 336Combined sources11
Helixi337 – 339Combined sources3
Beta strandi345 – 351Combined sources7
Helixi353 – 355Combined sources3
Beta strandi356 – 361Combined sources6
Beta strandi370 – 374Combined sources5
Helixi375 – 378Combined sources4
Turni379 – 381Combined sources3
Beta strandi393 – 397Combined sources5
Beta strandi406 – 412Combined sources7
Turni413 – 416Combined sources4
Beta strandi425 – 431Combined sources7
Helixi442 – 449Combined sources8
Turni461 – 464Combined sources4
Beta strandi470 – 481Combined sources12
Beta strandi484 – 490Combined sources7
Helixi491 – 493Combined sources3
Helixi504 – 514Combined sources11
Beta strandi518 – 529Combined sources12
Turni530 – 532Combined sources3
Helixi535 – 537Combined sources3
Beta strandi554 – 562Combined sources9
Helixi571 – 586Combined sources16
Beta strandi592 – 596Combined sources5
Helixi611 – 619Combined sources9
Turni620 – 624Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HM3X-ray2.25A2-637[»]
ProteinModelPortaliO53580.
SMRiO53580.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107RCI. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000266721.
InParanoidiO53580.
KOiK12428.
OMAiVDEWAVI.
PhylomeDBiO53580.

Family and domain databases

InterProiIPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O53580-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFVTGESGMA YHNPFIVNGK IRFPANTNLV RHVEKWAKVR GDKLAYRFLD
60 70 80 90 100
FSTERDGVAR DILWSDFSAR NRAVGARLQQ VTQPGDRVAI LCPQNLDYLI
110 120 130 140 150
SFFGALYSGR IAVPLFDPAE PGHVGRLHAV LDDCAPSTIL TTTDSAEGVR
160 170 180 190 200
KFIRARSAKE RPRVIAVDAV PTEVAATWQQ PEANEETVAY LQYTSGSTRI
210 220 230 240 250
PSGVQITHLN LPTNVVQVLN ALEGQEGDRG VSWLPFFHDM GLITVLLASV
260 270 280 290 300
LGHSFTFMTP AAFVRRPGRW IRELARKPGE TGGTFSAAPN FAFEHAAVRG
310 320 330 340 350
VPRDDEPPLD LSNVKGILNG SEPVSPASMR KFFEAFAPYG LKQTAVKPSY
360 370 380 390 400
GLAEATLFVS TTPMDEVPTV IHVDRDELNN QRFVEVAADA PNAVAQVSAG
410 420 430 440 450
KVGVSEWAVI VDADTASELP DGQIGEIWLH GNNLGTGYWG KEEESAQTFK
460 470 480 490 500
NILKSRISES RAEGAPDDAL WVRTGDYGTY FKDHLYIAGR IKDLVIIDGR
510 520 530 540 550
NHYPQDLECT AQESTKALRV GYAAAFSVPA NQLPQTVFDD SHAGLKFDPE
560 570 580 590 600
DTSEQLVIVG ERAAGTHKLD HQPIVDDIRA AIAVGHGVTV RDVLLVSAGT
610 620 630
IPRTSSGKIG RRACRAAYLD GSLRSGVGSP TVFATSD
Length:637
Mass (Da):69,232
Last modified:June 1, 1998 - v1
Checksum:i0A3A86CED9AE0EDC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46630.1.
PIRiE70887.
RefSeqiNP_218318.1. NC_000962.3.
WP_003899700.1. NC_000962.3.

Genome annotation databases

EnsemblBacteriaiCCP46630; CCP46630; Rv3801c.
GeneIDi886130.
KEGGimtu:Rv3801c.
mtv:RVBD_3801c.
PATRICi18157060. VBIMycTub87468_4232.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46630.1.
PIRiE70887.
RefSeqiNP_218318.1. NC_000962.3.
WP_003899700.1. NC_000962.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5HM3X-ray2.25A2-637[»]
ProteinModelPortaliO53580.
SMRiO53580.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3801c.

Chemistry databases

SwissLipidsiSLP:000000972.

Proteomic databases

PaxDbiO53580.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46630; CCP46630; Rv3801c.
GeneIDi886130.
KEGGimtu:Rv3801c.
mtv:RVBD_3801c.
PATRICi18157060. VBIMycTub87468_4232.

Organism-specific databases

TubercuListiRv3801c.

Phylogenomic databases

eggNOGiENOG4107RCI. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000266721.
InParanoidiO53580.
KOiK12428.
OMAiVDEWAVI.
PhylomeDBiO53580.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciMetaCyc:G185E-8097-MONOMER.
MTBH37RV:G185E-8097-MONOMER.

Family and domain databases

InterProiIPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFAA32_MYCTU
AccessioniPrimary (citable) accession number: O53580
Secondary accession number(s): L0TGT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: June 1, 1998
Last modified: November 30, 2016
This is version 96 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.