O28076 (FTR_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Formylmethanofuran--tetrahydromethanopterin formyltransferase
EC=2.3.1.101

Alternative name(s):
H4MPT formyltransferase

Gene names

Name:	ftr
Ordered Locus Names:	AF_2207

Organism

Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]

Taxonomic identifier

224325 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus › Archaeoglobus fulgidus

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of a formyl group from 5-formyl tetrahydromethanopterin (5-formyl-H4MPT) to methanofuran (MFR) so as to produce formylmethanofuran (formyl-MFR) and tetrahydromethanopterin (H4MPT). Ref.3
Catalytic activity	Formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin. HAMAP-Rule MF_00579
Pathway	Metabolic intermediate metabolism; lactate oxidation. HAMAP-Rule MF_00579
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the FTR family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	lactate oxidation Inferred from electronic annotation. Source: UniProtKB-UniPathway one-carbon metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	formylmethanofuran-tetrahydromethanopterin N-formyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 297

297

Formylmethanofuran--tetrahydromethanopterin formyltransferase HAMAP-Rule MF_00579

PRO_0000138115

Experimental info

Sequence conflict

32

1

Missing AA sequence Ref.2

Sequence conflict

32

1

Missing AA sequence Ref.3

Sequence conflict

34

1

W → I AA sequence Ref.2

Sequence conflict

34

1

W → I AA sequence Ref.3

Sequence conflict

43

1

F → T AA sequence Ref.3

Secondary structure

1

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297

Helix Strand Turn

Details...

Beta strand

6 – 8

3

Beta strand

12 – 26

15

Helix

30 – 41

12

Turn

47 – 49

3

Beta strand

53 – 60

8

Helix

62 – 64

3

Beta strand

71 – 80

10

Helix

81 – 95

15

Turn

96 – 98

3

Beta strand

103 – 107

5

Beta strand

112 – 115

4

Helix

117 – 121

5

Helix

122 – 125

4

Beta strand

130 – 134

5

Beta strand

137 – 143

7

Beta strand

145 – 153

9

Beta strand

155 – 172

18

Helix

173 – 188

16

Helix

198 – 200

3

Beta strand

202 – 204

3

Beta strand

207 – 209

3

Helix

222 – 224

3

Helix

226 – 228

3

Helix

229 – 232

4

Beta strand

243 – 253

11

Helix

254 – 268

15

Beta strand

274 – 278

5

Turn

283 – 285

3

Beta strand

288 – 292

5

Helix

293 – 295

3

Sequences

	Sequence		Length	Mass (Da)
	O28076 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 1466551AFFE97E4C	FASTA	297	31,762
	10 20 30 40 50 60 MKVNGVEVEE TFAEAFDIKI ARVLITGYDY YWAWVAANEA TGFGTSVIMC PAEAGIEIKA 70 80 90 100 110 120 KPSETPDGRP GYYIQICHMS KKGLEEQLLA RLGQCVLTAP TTAVFNGLPD AEEKFDTGFK 130 140 150 160 170 180 LKFFADGYEK EVEVGGRKCW AVPMMEGDFI IENDIGYTNG IAGGNFFIMA ETQPSALAAA 190 200 210 220 230 240 KAAVDAISDV EGVITPFPGG IVASGSKVGA NKYKFLKAST NEKFAPSIRD QVEGTQIPEG 250 260 270 280 290 VKAVYEIVIN GLNADAIKEA TRVGILAATK IPGVVKITAG NYGGKLGKHI INLNELF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]	"Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri." Breitung J., Borner G., Scholz S., Linder D., Stetter K.O., Thauer R.K. Eur. J. Biochem. 210:971-981(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-48. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[3]	"Formylmethanofuran: tetrahydromethanopterin formyltransferase and N5,N10-methylenetetrahydromethanopterin dehydrogenase from the sulfate-reducing Archaeoglobus fulgidus: similarities with the enzymes from methanogenic Archaea." Schworer B., Breitung J., Klein A.R., Stetter K.O., Thauer R.K. Arch. Microbiol. 159:225-232(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-48, FUNCTION. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[4]	"Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship." Mamat B., Roth A., Grimm C., Ermler U., Tziatzios C., Schubert D., Thauer R.K., Shima S. Protein Sci. 11:2168-2178(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000782 Genomic DNA. Translation: AAB89046.1.

PIR

G69525.

RefSeq

NP_071032.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M5H	X-ray	2.00	A/B/C/D/E/F/G/H	1-297	[»]

ProteinModelPortal

O28076.

SMR

O28076. Positions 1-297.

ModBase

Search...

Protein-protein interaction databases

STRING

224325.AF2207.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAB89046; AAB89046; AF_2207.

GeneID

1485436.

KEGG

afu:AF2207.

Phylogenomic databases

eggNOG

COG2037.

KO

K00672.

OMA

CPAEAGI.

ProtClustDB

PRK02114.

Enzyme and pathway databases

BioCyc

AFUL224325:GJBC-2252-MONOMER.

UniPathway

UPA00701.

Family and domain databases

Gene3D

3.30.70.520. 2 hits.

HAMAP

MF_00579. FTR.

InterPro

IPR014053. ForMFR_H4MPT_ForTrfase.
IPR002770. ForMFR_H4MPT_ForTrfase_C.
IPR023447. ForMFR_H4MPT_ForTrfase_fd-like.
IPR022667. ForMFR_H4MPT_ForTrfase_N.
[Graphical view]

Pfam

PF01913. FTR. 1 hit.
PF02741. FTR_C. 1 hit.
[Graphical view]

PIRSF

PIRSF006414. Ftr_formyl_trnsf. 1 hit.

SUPFAM

SSF55112. FTR_trans. 2 hits.

TIGRFAMs

TIGR03119. one_C_fhcD. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O28076.

Entry information

Entry name

FTR_ARCFU

Accession

Primary (citable) accession number: O28076

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program