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P29251

- FOL1_PNECA

UniProt

P29251 - FOL1_PNECA

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Protein

Folic acid synthesis protein fol1

Gene

fol1

Organism
Pneumocystis carinii
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Mg2+By similarityNote: Binds 1 Mg(2+) ion per subunit. Magnesium is required for activity, even if it interacts primarily with the substrate.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
Complete GO annotation...

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

        10         20         30         40         50
MIFKSLKIFP FYQIYGFRFL KGMIFKKKIH LSKLNKNHDL IHIHSLTLKS
60 70 80 90 100
IVGKNSWAQR LLQPVVLTLS MGINASLSGN MDDLSYSIDY ATVYKEVFKL
110 120 130 140 150
VENSKFENLL DLSDKISKVV LGDKCKGNWV KVIAETPKGH LLAETGLQII
160 170 180 190 200
RRKDGIREID DQFFIKNLSL YTIIGINPEE RVNKQNIIID LILFKSSINL
210 220 230 240 250
ECKDDFIINT YNIEKLLKEI VKHVEESTFK TIEALALSIA RISCISHNIE
260 270 280 290 300
KIIVKVKKSC ALAFAESAGV EIVRSRSCFS SNNYIKSENS IDNEAVYISL
310 320 330 340 350
GSNLGNRIKF ILDAIEKMSI KGIKVLKTSM LYESKPMYFK DQPAFYNAVC
360 370 380 390 400
KVQTSLHPEQ LLFELQLIEK ELGRVKVIDK GPRCIDLDIV FYGRKIINSE
410 420 430 440 450
SLIIPHPRVL ERSFVLKPLL DISGDLVHPV TGLSIASYFE KIVDHDIKPV
460 470 480 490 500
LPFLYKNKSI DFSFRSYKAP TYIMAILNLT PDSFFDGGIH SYDSVLIDVE
510 520 530 540 550
KFINAGATII DIGGQSTRPG SYIIPLEEEI FRVIPAIKYL QKTYPDILIS
560 570 580 590 600
IDTFRSEVAE QAVKAGASLV NDISGGRYDP KMFNTVARLK VPICIMHMRG
610 620 630 640 650
NFLNMDNLTD YGTDIIEQIT IELEKLLNSA EKSGIPRWNI ILDPGLGFSK
660 670 680 690 700
TLHQNIELLR RFNELKSKNC FNGLPWLLGP SRKRFTGFIT GDNMPKDRIW
710 720 730 740
GTVAAVVASI SGGCDIIRVH DVYEMYKISK MSDAIWKEIY
Length:740
Mass (Da):83,962
Last modified:December 1, 1992 - v1
Checksum:i328F6EB91B4499EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86602 Genomic DNA. Translation: AAA33790.1.
PIRiS28666.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 85 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