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Q5RCH4

- FAD1_PONAB

UniProt

Q5RCH4 - FAD1_PONAB

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
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    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

    GO - Biological processi

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

    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

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 491491FAD synthasePRO_0000302739Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiQ5RCH4.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5RCH4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni17 – 10892Molybdenum cofactor biosynthesis protein-likeAdd
    BLAST
    Regioni302 – 459158FAD synthaseAdd
    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.Curated
    In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily.Curated

    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...
    MobiDBi 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: October 1, 2014
    This is version 54 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