Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P29251

- FOL1_PNECA

UniProt

P29251 - FOL1_PNECA

Protein

Folic acid synthesis protein fol1

Gene

fol1

Organism
Pneumocystis carinii
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes three sequential steps of tetrahydrofolate biosynthesis.1 Publication

    Catalytic activityi

    2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde.
    ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = AMP + (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate.
    (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.

    Cofactori

    Binds 1 magnesium ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate By similarity.By similarity

    Kineticsi

    1. KM=2.3 µM for 7,8-dihydroneopterin2 Publications
    2. KM=3.6 µM for 6-hydroxymethyl-7,8-dihydropterin2 Publications

    Vmax=36 nmol/min/mg enzyme for 7,8-dihydroneopterin2 Publications

    pH dependencei

    Optimum pH is 8.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi478 – 4781MagnesiumBy similarity
    Binding sitei486 – 4861SubstrateBy similarity
    Binding sitei552 – 5521SubstrateBy similarity
    Binding sitei571 – 5711SubstrateBy similarity
    Binding sitei643 – 6431SubstrateBy similarity
    Binding sitei683 – 6831SubstrateBy similarity
    Binding sitei718 – 7181SubstrateBy similarity
    Binding sitei720 – 7201SubstrateBy similarity

    GO - Molecular functioni

    1. 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity Source: UniProtKB-EC
    2. ATP binding Source: UniProtKB-KW
    3. dihydroneopterin aldolase activity Source: UniProtKB-EC
    4. dihydropteroate synthase activity Source: UniProtKB-EC
    5. kinase activity Source: UniProtKB-KW
    6. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. folic acid biosynthetic process Source: UniProtKB-KW
    2. tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Kinase, Lyase, Transferase

    Keywords - Biological processi

    Folate biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKP29251.
    UniPathwayiUPA00077; UER00154.
    UPA00077; UER00155.
    UPA00077; UER00156.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Folic acid synthesis protein fol1
    Including the following 3 domains:
    Dihydroneopterin aldolase (EC:4.1.2.25)
    Short name:
    DHNA
    Alternative name(s):
    FASA
    FASB
    2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (EC:2.7.6.3)
    Alternative name(s):
    6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
    Short name:
    PPPK
    7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
    Short name:
    HPPK
    FASC
    Dihydropteroate synthase (EC:2.5.1.15)
    Short name:
    DHPS
    Alternative name(s):
    Dihydropteroate pyrophosphorylase
    FASD
    Gene namesi
    Name:fol1
    Synonyms:fas
    OrganismiPneumocystis carinii
    Taxonomic identifieri4754 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaPneumocystidomycetesPneumocystidaceaePneumocystis

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi39 – 391D → E: Abolishes DHNA activity. 1 Publication
    Mutagenesisi53 – 531G → A: Reduces DHNA activity 11-fold. 1 Publication
    Mutagenesisi63 – 631Q → N: Reduces DHNA activity 16-fold. 1 Publication
    Mutagenesisi161 – 1611D → E: No effect. 1 Publication
    Mutagenesisi175 – 1751G → A: Abolishes DHNA activity. 1 Publication
    Mutagenesisi185 – 1851Q → N: Reduces DHNA activity 24-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 740740Folic acid synthesis protein fol1PRO_0000168242Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP29251.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini471 – 730260Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni39 – 160122DHNA 1Add
    BLAST
    Regioni161 – 280120DHNA 2Add
    BLAST
    Regioni291 – 449159HPPKAdd
    BLAST
    Regioni463 – 740278DHPSAdd
    BLAST
    Regioni517 – 5182Substrate bindingBy similarity

    Sequence similaritiesi

    In the N-terminal section; belongs to the DHNA family.Curated
    In the central section; belongs to the HPPK family.Curated
    In the C-terminal section; belongs to the DHPS family.Curated
    Contains 1 pterin-binding domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di3.20.20.20. 1 hit.
    3.30.70.560. 1 hit.
    InterProiIPR006390. DHP_synth.
    IPR011005. Dihydropteroate_synth-like.
    IPR006157. FolB_dom.
    IPR016261. Folic_acid_synth.
    IPR000550. Hppk.
    IPR000489. Pterin-binding.
    [Graphical view]
    PfamiPF02152. FolB. 2 hits.
    PF01288. HPPK. 1 hit.
    PF00809. Pterin_bind. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000741. Folic_acid_synth. 1 hit.
    SMARTiSM00905. FolB. 2 hits.
    [Graphical view]
    SUPFAMiSSF51717. SSF51717. 1 hit.
    SSF55083. SSF55083. 1 hit.
    TIGRFAMsiTIGR01496. DHPS. 1 hit.
    TIGR00526. folB_dom. 2 hits.
    TIGR01498. folK. 1 hit.
    PROSITEiPS00792. DHPS_1. 1 hit.
    PS00793. DHPS_2. 1 hit.
    PS00794. HPPK. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P29251-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIFKSLKIFP FYQIYGFRFL KGMIFKKKIH LSKLNKNHDL IHIHSLTLKS    50
    IVGKNSWAQR LLQPVVLTLS MGINASLSGN MDDLSYSIDY ATVYKEVFKL 100
    VENSKFENLL DLSDKISKVV LGDKCKGNWV KVIAETPKGH LLAETGLQII 150
    RRKDGIREID DQFFIKNLSL YTIIGINPEE RVNKQNIIID LILFKSSINL 200
    ECKDDFIINT YNIEKLLKEI VKHVEESTFK TIEALALSIA RISCISHNIE 250
    KIIVKVKKSC ALAFAESAGV EIVRSRSCFS SNNYIKSENS IDNEAVYISL 300
    GSNLGNRIKF ILDAIEKMSI KGIKVLKTSM LYESKPMYFK DQPAFYNAVC 350
    KVQTSLHPEQ LLFELQLIEK ELGRVKVIDK GPRCIDLDIV FYGRKIINSE 400
    SLIIPHPRVL ERSFVLKPLL DISGDLVHPV TGLSIASYFE KIVDHDIKPV 450
    LPFLYKNKSI DFSFRSYKAP TYIMAILNLT PDSFFDGGIH SYDSVLIDVE 500
    KFINAGATII DIGGQSTRPG SYIIPLEEEI FRVIPAIKYL QKTYPDILIS 550
    IDTFRSEVAE QAVKAGASLV NDISGGRYDP KMFNTVARLK VPICIMHMRG 600
    NFLNMDNLTD YGTDIIEQIT IELEKLLNSA EKSGIPRWNI ILDPGLGFSK 650
    TLHQNIELLR RFNELKSKNC FNGLPWLLGP SRKRFTGFIT GDNMPKDRIW 700
    GTVAAVVASI SGGCDIIRVH DVYEMYKISK MSDAIWKEIY 740
    Length:740
    Mass (Da):83,962
    Last modified:December 1, 1992 - v1
    Checksum:i328F6EB91B4499EB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86602 Genomic DNA. Translation: AAA33790.1.
    PIRiS28666.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86602 Genomic DNA. Translation: AAA33790.1 .
    PIRi S28666.

    3D structure databases

    ProteinModelPortali P29251.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00077 ; UER00154 .
    UPA00077 ; UER00155 .
    UPA00077 ; UER00156 .
    SABIO-RK P29251.

    Family and domain databases

    Gene3Di 3.20.20.20. 1 hit.
    3.30.70.560. 1 hit.
    InterProi IPR006390. DHP_synth.
    IPR011005. Dihydropteroate_synth-like.
    IPR006157. FolB_dom.
    IPR016261. Folic_acid_synth.
    IPR000550. Hppk.
    IPR000489. Pterin-binding.
    [Graphical view ]
    Pfami PF02152. FolB. 2 hits.
    PF01288. HPPK. 1 hit.
    PF00809. Pterin_bind. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000741. Folic_acid_synth. 1 hit.
    SMARTi SM00905. FolB. 2 hits.
    [Graphical view ]
    SUPFAMi SSF51717. SSF51717. 1 hit.
    SSF55083. SSF55083. 1 hit.
    TIGRFAMsi TIGR01496. DHPS. 1 hit.
    TIGR00526. folB_dom. 2 hits.
    TIGR01498. folK. 1 hit.
    PROSITEi PS00792. DHPS_1. 1 hit.
    PS00793. DHPS_2. 1 hit.
    PS00794. HPPK. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The multifunctional folic acid synthesis fas gene of Pneumocystis carinii appears to encode dihydropteroate synthase and hydroxymethyldihydropterin pyrophosphokinase."
      Volpes F., Dyer M., Scaife J.G., Darby G., Stammers D.K., Delves C.J.
      Gene 112:213-218(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The multifunctional folic acid synthesis fas gene of Pneumocystis carinii encodes dihydroneopterin aldolase, hydroxymethyldihydropterin pyrophosphokinase and dihydropteroate synthase."
      Volpe F., Ballantine S.P., Delves C.J.
      Eur. J. Biochem. 216:449-458(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    3. "The hydroxymethyldihydropterin pyrophosphokinase domain of the multifunctional folic acid synthesis Fas protein of Pneumocystis carinii expressed as an independent enzyme in Escherichia coli: refolding and characterization of the recombinant enzyme."
      Ballantine S.P., Volpe F., Delves C.J.
      Protein Expr. Purif. 5:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY.
    4. "Two domains with amino-acid sequence similarity are required for dihydroneopterin aldolase function in the multifunctional folic acid synthesis Fas protein of Pneumocystis carinii."
      Volpe F., Ballantine S.P., Delves C.J.
      Gene 160:41-46(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    5. "Single amino acid substitutions disrupt tetramer formation in the dihydroneopterin aldolase enzyme of Pneumocystis carinii."
      Thomas M.C., Ballantine S.P., Bethell S.S., Bains S., Kellam P., Delves C.J.
      Biochemistry 37:11629-11636(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-39; GLY-53; GLN-63; ASP-161; GLY-175 AND GLN-185.

    Entry informationi

    Entry nameiFOL1_PNECA
    AccessioniPrimary (citable) accession number: P29251
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Multifunctional enzyme

    Documents

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

    External Data

    Dasty 3