Q2GI30 (Q2GI30_EHRCR) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Peptide deformylase 1 HAMAP MF_00163
Short name=PDF 1 HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163

Alternative name(s):
Polypeptide deformylase 1 HAMAP MF_00163

Gene names

Name:	def EMBL ABD45529.1
Synonyms:	def1 HAMAP MF_00163
Ordered Locus Names:	ECH_0073

Organism

Ehrlichia chaffeensis (strain Arkansas) [Complete proteome] [HAMAP]

Taxonomic identifier

205920 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Ehrlichia

Protein attributes

Sequence length	188 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. HAMAP MF_00163
Catalytic activity	Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP MF_00163 SAAS SAAS000181
Cofactor	Binds 1 Fe2+ ion By similarity. HAMAP MF_00163
Sequence similarities	Belongs to the polypeptide deformylase family. HAMAP MF_00163 RuleBase RU003335

Ontologies

Keywords
Biological process	Protein biosynthesis SAAS SAAS000181 HAMAP MF_00163
Ligand	Iron HAMAP MF_00163 Metal-binding HAMAP MF_00163 SAAS SAAS000181 PDB 3OCA Zinc PDB 3OCA
Molecular function	Hydrolase HAMAP MF_00163 SAAS SAAS000181 EMBL ABD45529.1
Technical term	3D-structure PDB 3OCA Complete proteome
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: HAMAP
Molecular function	iron ion binding Inferred from electronic annotation. Source: InterPro peptide deformylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	154	1	By similarity HAMAP MF_00163
	Metal binding	111	1	Iron By similarity HAMAP MF_00163
	Metal binding	111	1	Zinc PDB 3OCA
	Metal binding	153	1	Iron By similarity HAMAP MF_00163
	Metal binding	153	1	Zinc; via tele nitrogen PDB 3OCA
	Metal binding	157	1	Iron By similarity HAMAP MF_00163
	Metal binding	157	1	Zinc; via tele nitrogen PDB 3OCA

Sequences

	Sequence		Length	Mass (Da)
	Q2GI30 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: 55D3DCF040A0D3ED	FASTA	188	21,568
	10 20 30 40 50 60 MSVLSIVTVP DKRLSLCSEE VEKVDQSIRK LVDDMFETMH ANQGLGLAAV QVGVHKRILV 70 80 90 100 110 120 MNVPEEFEDS EDIENVEDKI EGYELYGGPY CIINPKIVDI SQEKVKLKEG CLSVPGYFDY 130 140 150 160 170 180 IVRPQRIAVQ YLDYNGNECI IKAQGWLARC LQHEIDHLNG TVFLKYLSKF KRDFAIEKVK KKERTDLI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. , Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H. PLoS Genet. 2:208-222(2006) [PubMed: 16482227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Crystal structure of peptide deformylase from Ehrlichia chaffeensis." Seattle Structural Genomics Center for Infectious Disease (SSGCID) Abendroth J., Sankaran B., Edwards T.E., Staker B. Submitted (AUG-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZINC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000236 Genomic DNA. Translation: ABD45529.1.

RefSeq

YP_506903.1. NC_007799.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3OCA	X-ray	2.40	A/B	1-188	[»]
3U04	X-ray	1.70	A	1-188	[»]

ProteinModelPortal

Q2GI30.

ModBase

Search...

Protein-protein interaction databases

STRING

Q2GI30.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3927935.

GenomeReviews

Gene locus ECH_0073 in contig CP000236_GR.

KEGG

ech:ECH_0073.

PATRIC

20575709. VBIEhrCha103583_0064.

TIGR

ECH_0073.

Phylogenomic databases

eggNOG

COG0242.

HOGENOM

HBG665227.

OMA

PLKRQRM.

PhylomeDB

Q2GI30.

ProtClustDB

CLSK749063.

Family and domain databases

HAMAP

MF_00163. Pep_deformylase.
[Tree]

InterPro

IPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]

Gene3D

G3DSA:3.90.45.10. Fmet_deformylase. 1 hit.

KO

K01462.

PANTHER

PTHR10458. Fmet_deformylase. 1 hit.

Pfam

PF01327. Pep_deformylase. 1 hit.
[Graphical view]

PIRSF

PIRSF004749. Pep_def. 1 hit.

PRINTS

PR01576. PDEFORMYLASE.

SUPFAM

SSF56420. Fmet_deformylase. 1 hit.

TIGRFAMs

TIGR00079. Pept_deformyl. 1 hit.

ProtoNet

Search...

Entry information

Entry name

Q2GI30_EHRCR

Accession

Primary (citable) accession number: Q2GI30

Entry history

Integrated into UniProtKB/TrEMBL:	March 21, 2006
Last sequence update:	March 21, 2006
Last modified:	December 14, 2011
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)