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Q2RK25

- DEF_MOOTA

UniProt

Q2RK25 - DEF_MOOTA

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Protein

Peptide deformylase

Gene
def, Moth_0897
Organism
Moorella thermoacetica (strain ATCC 39073)
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions By similarity.UniRule annotation

Catalytic activityi

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide.UniRule annotation

Cofactori

Binds 1 Fe2+ ion By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi88 – 881Iron By similarity
Metal bindingi130 – 1301Iron By similarity
Active sitei131 – 1311 By similarity
Metal bindingi134 – 1341Iron By similarity

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. peptide deformylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMTHE264732:GH0A-934-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide deformylase (EC:3.5.1.88)
Short name:
PDF
Alternative name(s):
Polypeptide deformylase
Gene namesi
Name:def
Ordered Locus Names:Moth_0897
OrganismiMoorella thermoacetica (strain ATCC 39073)
Taxonomic identifieri264732 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella
ProteomesiUP000007053: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 155155Peptide deformylaseUniRule annotationPRO_0000301056Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi264732.Moth_0897.

Structurei

3D structure databases

ProteinModelPortaliQ2RK25.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243508.
KOiK01462.
OMAiELLAICI.
OrthoDBiEOG664CMF.

Family and domain databases

Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase.
InterProiIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFiPIRSF004749. Pep_def. 1 hit.
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.

Sequencei

Sequence statusi: Complete.

Q2RK25-1 [UniParc]FASTAAdd to Basket

« Hide

MAIHKILTLG DPLLREKSQP VRKITSNVWK LLDNLADTMY DAPGVGLAAP    50
QIGVLKRVIV VDVGEGLTEL INPEVIAASG EEVGAEGCLS IPGAQGEVPR 100
AAVVTVRGLD RHGRVREIRA EGLYARALQH EIDHLDGILF IDKVVRWLEN 150
QPGER 155
Length:155
Mass (Da):16,851
Last modified:January 24, 2006 - v1
Checksum:i9F0415CE4692EF7F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000232 Genomic DNA. Translation: ABC19214.1.
RefSeqiWP_011392416.1. NC_007644.1.
YP_429757.1. NC_007644.1.

Genome annotation databases

EnsemblBacteriaiABC19214; ABC19214; Moth_0897.
GeneIDi3831439.
KEGGimta:Moth_0897.
PATRICi22638956. VBIMooThe6753_0965.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000232 Genomic DNA. Translation: ABC19214.1 .
RefSeqi WP_011392416.1. NC_007644.1.
YP_429757.1. NC_007644.1.

3D structure databases

ProteinModelPortali Q2RK25.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 264732.Moth_0897.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC19214 ; ABC19214 ; Moth_0897 .
GeneIDi 3831439.
KEGGi mta:Moth_0897.
PATRICi 22638956. VBIMooThe6753_0965.

Phylogenomic databases

eggNOGi COG0242.
HOGENOMi HOG000243508.
KOi K01462.
OMAi ELLAICI.
OrthoDBi EOG664CMF.

Enzyme and pathway databases

BioCyci MTHE264732:GH0A-934-MONOMER.

Family and domain databases

Gene3Di 3.90.45.10. 1 hit.
HAMAPi MF_00163. Pep_deformylase.
InterProi IPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view ]
PANTHERi PTHR10458. PTHR10458. 1 hit.
Pfami PF01327. Pep_deformylase. 1 hit.
[Graphical view ]
PIRSFi PIRSF004749. Pep_def. 1 hit.
PRINTSi PR01576. PDEFORMYLASE.
SUPFAMi SSF56420. SSF56420. 1 hit.
TIGRFAMsi TIGR00079. pept_deformyl. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39073.

Entry informationi

Entry nameiDEF_MOOTA
AccessioniPrimary (citable) accession number: Q2RK25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 24, 2006
Last modified: September 3, 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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