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Q5RCH4

- FAD1_PONAB

UniProt

Q5RCH4 - FAD1_PONAB

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Protein
FAD synthase
Gene
FLAD1
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme By similarity.

Catalytic activityi

ATP + FMN = diphosphate + FAD.

Cofactori

Magnesium By similarity.

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. FMN adenylyltransferase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. FAD biosynthetic process Source: UniProtKB-UniPathway
  2. Mo-molybdopterin cofactor biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, FAD, Flavoprotein, FMN, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00277; UER00407.

Names & Taxonomyi

Protein namesi
Recommended name:
FAD synthase (EC:2.7.7.2)
Alternative name(s):
FAD pyrophosphorylase
FMN adenylyltransferase
Flavin adenine dinucleotide synthase
Including the following 2 domains:
Molybdenum cofactor biosynthesis protein-like region
FAD synthase region
Gene namesi
Name:FLAD1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491FAD synthase
PRO_0000302739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine By similarity
Modified residuei282 – 2821N6-acetyllysine; alternate By similarity
Modified residuei282 – 2821N6-succinyllysine; alternate By similarity
Modified residuei467 – 4671Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ5RCH4.

Structurei

3D structure databases

ProteinModelPortaliQ5RCH4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni17 – 10892Molybdenum cofactor biosynthesis protein-like
Add
BLAST
Regioni302 – 459158FAD synthase
Add
BLAST

Domaini

The molybdenum cofactor biosynthesis protein-like region may not be functional.

Sequence similaritiesi

In the N-terminal section; belongs to the MoaB/Mog family.
In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily.

Phylogenomic databases

HOVERGENiHBG058211.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.40.980.10. 1 hit.
InterProiIPR012183. FAD_synth_Mopterin-bd.
IPR001453. Mopterin-bd_dom.
IPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 1 hit.
PF01507. PAPS_reduct. 2 hits.
[Graphical view]
PIRSFiPIRSF036620. MPTbdFAD. 1 hit.
SMARTiSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5RCH4-1 [UniParc]FASTAAdd to Basket

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MTSRASELSP GRSVTAGIII VGDEILKGHT QDTNTFFLCR TLRSLGVQVC    50
RVSVAPDEVA TIAAEVTSFS NRFTHVLTAG GIGPTHDDVT FEAVAQAFGD 100
ELKPHPELEA ATKALGGEGW EKLSLVPSSA CLHYGTDPRT GHPFRFPLVS 150
VRNVYLFPSI PELLRRVLEG MKGLFQNPAV QFHSKELYVA ADEASIAPIL 200
AEAQAHFGRR LGLGSYPDWG SNYYQVKLTL DSRGRRIPGG NAWPNLTARL 250
PQGSLVPYMP NAVEQASEAV YKLAESGSSL GKKVAGALQT IETALAQYSL 300
TQLCVGFNGG KDCTALLHLF HAAVQRKLPD VPNPLQILYI RSISPFPELE 350
QFLQDTIKRY NLQMLEAEGS MKQALGELQA RHPQLEAVLM GTRRTDPYSC 400
SLCPFSPTDP GWPAFMRINP LLDWTYRDIW DFLRQLFVPY CILYDRGYTS 450
LGSRENTVRD PALKRLSPGG HPTYRPAYLL ENEEEERNSR T 491
Length:491
Mass (Da):54,307
Last modified:December 21, 2004 - v1
Checksum:iBD18AD9F84592F52
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR858296 mRNA. Translation: CAH90533.1.
UniGeneiPab.13439.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR858296 mRNA. Translation: CAH90533.1 .
UniGenei Pab.13439.

3D structure databases

ProteinModelPortali Q5RCH4.
ModBasei Search...

Proteomic databases

PRIDEi Q5RCH4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG058211.

Enzyme and pathway databases

UniPathwayi UPA00277 ; UER00407 .

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
3.40.980.10. 1 hit.
InterProi IPR012183. FAD_synth_Mopterin-bd.
IPR001453. Mopterin-bd_dom.
IPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
Pfami PF00994. MoCF_biosynth. 1 hit.
PF01507. PAPS_reduct. 2 hits.
[Graphical view ]
PIRSFi PIRSF036620. MPTbdFAD. 1 hit.
SMARTi SM00852. MoCF_biosynth. 1 hit.
[Graphical view ]
SUPFAMi SSF53218. SSF53218. 1 hit.
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiFAD1_PONAB
AccessioniPrimary (citable) accession number: Q5RCH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 21, 2004
Last modified: March 19, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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