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Q5F9K6

- GCH4_NEIG1

UniProt

Q5F9K6 - GCH4_NEIG1

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Protein

GTP cyclohydrolase FolE2

Gene

folE2

Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Converts GTP to 7,8-dihydroneopterin triphosphate.1 Publication

Catalytic activityi

GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei147 – 1471May be catalytically importantBy similarity

GO - Molecular functioni

  1. GTP cyclohydrolase I activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 7,8-dihydroneopterin 3'-triphosphate biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciNGON242231:GI2G-366-MONOMER.
UniPathwayiUPA00848; UER00151.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP cyclohydrolase FolE2 (EC:3.5.4.16)
Alternative name(s):
GTP cyclohydrolase 1B
Gene namesi
Name:folE2
Ordered Locus Names:NGO0387
OrganismiNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Taxonomic identifieri242231 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000535: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257GTP cyclohydrolase FolE2PRO_0000147714Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi242231.NGO0387.

Structurei

Secondary structure

1
257
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 3417Combined sources
Beta strandi37 – 5115Combined sources
Helixi61 – 699Combined sources
Helixi76 – 8914Combined sources
Beta strandi93 – 10816Combined sources
Turni110 – 1123Combined sources
Beta strandi115 – 12915Combined sources
Beta strandi132 – 14615Combined sources
Helixi148 – 1536Combined sources
Beta strandi154 – 1563Combined sources
Beta strandi160 – 17314Combined sources
Helixi177 – 1859Combined sources
Beta strandi188 – 1914Combined sources
Helixi198 – 21013Combined sources
Helixi215 – 22814Combined sources
Beta strandi232 – 24110Combined sources
Beta strandi246 – 25611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3D1TX-ray2.20A/B1-257[»]
3D2OX-ray2.04A/B1-257[»]
ProteinModelPortaliQ5F9K6.
SMRiQ5F9K6. Positions 15-256.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5F9K6.

Family & Domainsi

Sequence similaritiesi

Belongs to the GTP cyclohydrolase IV family.Curated

Phylogenomic databases

eggNOGiCOG1469.
HOGENOMiHOG000280679.
KOiK09007.
OMAiDVQSSRD.
OrthoDBiEOG6X6RBH.

Family and domain databases

HAMAPiMF_01527_B. GTP_cyclohydrol_B.
InterProiIPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view]
PfamiPF02649. GCHY-1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00294. TIGR00294. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5F9K6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNAIADVQSS RDLRNLPINQ VGIKDLRFPI TLKTAEGTQS TVARLTMTVY
60 70 80 90 100
LPAEQKGTHM SRFVALMEQH TEVLDFAQLH RLTAEMVALL DSRAGKISVS
110 120 130 140 150
FPFFRKKTAP VSGIRSLLDY DVSLTGEMKD GAYGHSMKVM IPVTSLCPCS
160 170 180 190 200
KEISQYGAHN QRSHVTVSLT SDAEVGIEEV IDYVETQASC QLYGLLKRPD
210 220 230 240 250
EKYVTEKAYE NPKFVEDMVR DVATSLIADK RIKSFVVESE NFESIHNHSA

YAYIAYP
Length:257
Mass (Da):28,747
Last modified:March 15, 2005 - v1
Checksum:iA0235399C3EDF2A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004969 Genomic DNA. Translation: AAW89131.1.
RefSeqiYP_207543.1. NC_002946.2.

Genome annotation databases

EnsemblBacteriaiAAW89131; AAW89131; NGO0387.
GeneIDi3282560.
KEGGingo:NGO0387.
PATRICi20333781. VBINeiGon24812_0468.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004969 Genomic DNA. Translation: AAW89131.1 .
RefSeqi YP_207543.1. NC_002946.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3D1T X-ray 2.20 A/B 1-257 [» ]
3D2O X-ray 2.04 A/B 1-257 [» ]
ProteinModelPortali Q5F9K6.
SMRi Q5F9K6. Positions 15-256.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 242231.NGO0387.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAW89131 ; AAW89131 ; NGO0387 .
GeneIDi 3282560.
KEGGi ngo:NGO0387.
PATRICi 20333781. VBINeiGon24812_0468.

Phylogenomic databases

eggNOGi COG1469.
HOGENOMi HOG000280679.
KOi K09007.
OMAi DVQSSRD.
OrthoDBi EOG6X6RBH.

Enzyme and pathway databases

UniPathwayi UPA00848 ; UER00151 .
BioCyci NGON242231:GI2G-366-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q5F9K6.

Family and domain databases

HAMAPi MF_01527_B. GTP_cyclohydrol_B.
InterProi IPR022838. GTP_cyclohydrolase_FolE2.
IPR003801. GTP_cyclohydrolase_FolE2/MptA.
[Graphical view ]
Pfami PF02649. GCHY-1. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00294. TIGR00294. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of Neisseria gonorrhoeae."
    Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H.
    , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700825 / FA 1090.
  2. Cited for: FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiGCH4_NEIG1
AccessioniPrimary (citable) accession number: Q5F9K6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: March 15, 2005
Last modified: November 26, 2014
This is version 58 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3