O88618 (FTCD_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Formimidoyltransferase-cyclodeaminase

Alternative name(s):
58 kDa microtubule-binding protein
Formiminotransferase-cyclodeaminase
Short name=FTCD

Including the following 2 domains:

1. Glutamate formimidoyltransferase
   EC=2.1.2.5
   Alternative name(s):
   Glutamate formiminotransferase
   Glutamate formyltransferase
2. Formimidoyltetrahydrofolate cyclodeaminase
   EC=4.3.1.4
   Alternative name(s):
   Formiminotetrahydrofolate cyclodeaminase

Gene names

Name:

Ftcd

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	541 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool By similarity. Ref.5 Binds and promotes bundling of vimentin filaments originating from the Golgi. Ref.5
Catalytic activity	5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate. 5-formyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formyl-L-glutamate. 5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3.
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid degradation; L-histidine degradation into L-glutamate; L-glutamate from N-formimidoyl-L-glutamate (transferase route): step 1/1. One-carbon metabolism; tetrahydrofolate interconversion.
Subunit structure	Homooctamer, including four polyglutamate binding sites. The subunits are arranged as a tetramer of dimers, and form a planar ring-shaped structure. Ref.6 Ref.7
Subcellular location	Cytoplasm › cytoskeleton › centrosome › centriole By similarity. Golgi apparatus. Note: More abundantly located around the mother centriole By similarity. Ref.4 Ref.5
Tissue specificity	Liver.
Sequence similarities	In the C-terminal section; belongs to the cyclodeaminase/cyclohydrolase family. In the N-terminal section; belongs to the formiminotransferase family.

Ontologies

Keywords
Biological process	Histidine metabolism
Cellular component	Cytoplasm Cytoskeleton Golgi apparatus
Ligand	Folate-binding Pyridoxal phosphate
Molecular function	Lyase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	cytoskeleton organization Inferred from mutant phenotype Ref.5. Source: RGD histidine catabolic process to glutamate and formamide Inferred from electronic annotation. Source: UniProtKB-UniPathway histidine catabolic process to glutamate and formate Inferred from electronic annotation. Source: UniProtKB-UniPathway tetrahydrofolate interconversion Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi apparatus Inferred from direct assay Ref.3. Source: RGD centriole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	folic acid binding Inferred from electronic annotation. Source: UniProtKB-KW formimidoyltetrahydrofolate cyclodeaminase activity Traceable author statement Ref.5. Source: RGD glutamate formimidoyltransferase activity Traceable author statement Ref.5. Source: RGD intermediate filament binding Traceable author statement Ref.5. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 541

541

Formimidoyltransferase-cyclodeaminase

PRO_0000087362

Regions

Region

1 – 181

181

Formiminotransferase N-subdomain

Region

163 – 172

10

Folate binding Potential

Region

182 – 326

145

Formiminotransferase C-subdomain

Region

327 – 334

8

Linker

Region

335 – 541

207

Cyclodeaminase/cyclohydrolase

Sites

Active site

82

1

For formimidoyltransferase activity By similarity

Active site

412

1

For cyclodeaminase activity Probable

Amino acid modifications

Modified residue

519

1

Phosphoserine By similarity

Secondary structure

1

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541

Helix Strand Turn

Details...

Beta strand

4 – 7

4

Helix

17 – 26

10

Turn

27 – 29

3

Beta strand

33 – 41

9

Turn

42 – 45

4

Beta strand

46 – 53

8

Helix

55 – 70

16

Helix

75 – 77

3

Beta strand

86 – 88

3

Beta strand

90 – 98

9

Helix

101 – 119

19

Beta strand

123 – 127

5

Beta strand

135 – 137

3

Helix

138 – 141

4

Helix

149 – 152

4

Beta strand

156 – 158

3

Beta strand

161 – 163

3

Beta strand

174 – 178

5

Beta strand

183 – 191

9

Helix

193 – 203

11

Beta strand

208 – 212

5

Beta strand

219 – 226

8

Turn

227 – 230

4

Beta strand

231 – 239

9

Turn

241 – 243

3

Helix

246 – 258

13

Turn

259 – 261

3

Beta strand

264 – 271

8

Helix

275 – 289

15

Helix

296 – 305

10

Beta strand

310 – 313

4

Helix

317 – 320

4

Helix

322 – 325

4

Helix

335 – 337

3

Helix

340 – 347

8

Beta strand

352 – 354

3

Helix

357 – 377

21

Beta strand

379 – 381

3

Helix

385 – 387

3

Helix

388 – 406

19

Helix

408 – 423

16

Helix

430 – 432

3

Turn

433 – 435

3

Helix

436 – 468

33

Helix

477 – 502

26

Helix

508 – 539

32

Sequences

	Sequence		Length	Mass (Da)
	O88618 [UniParc]. Last modified June 6, 2002. Version 4. Checksum: 76D806CE23478D92	FASTA	541	58,914
	10 20 30 40 50 60 MSQLVECVPN FSEGNNQEVI DAISQAISQT PGCVLLDVDA GPSTNRTVYT FVGQPECVVE 70 80 90 100 110 120 GALSAARTAS QLIDMRKHKG EHPRMGALDV CPFIPVRGVS MDECVLCAKA FGQRLAEELN 130 140 150 160 170 180 VPVYLYGEAA QMPSRQTLPA IRAGEYEALP EKLKQAEWVP DFGPSSFVPS WGATVTGARK 190 200 210 220 230 240 FLIAFNINLL STKEQAHRIA LNLREQGRGK DQPGRLKKVQ GIGWYLEEKN LAQVSTNLLD 250 260 270 280 290 300 FEVTALHTVY EEARREAQEL NLPVVGSQLV GLVPLKALLD AAAFYCDKEK LFVLEEEHRI 310 320 330 340 350 360 RLVVNRLGLD SLAPFDPKER IIEYLVPDSG PEQSLLDASL RAFVREVGAR SAAPGGGSVA 370 380 390 400 410 420 AAVAALGAAL ASMVGQMTYG RRQFDHLDST MRRLIPPFHA ASAQLTSLVD ADARAFAACL 430 440 450 460 470 480 GAIKLPKNTP EERDRRTCAL QEGLRQAVAV PLKLAETVSQ LWPALQELAQ CGNLSCLSDL 490 500 510 520 530 540 QVAAKALETG VFGAYFNVLI NLKDMTDDVF KEKTRHRISS LLQEAKTQAA LVLGSLEARK E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Gao Y.-S., Sztul E. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION TO 257. Strain: Sprague-Dawley. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[3]	"Molecular cloning, characterization, and dynamics of rat formiminotransferase cyclodeaminase, a Golgi-associated 58-kDa protein." Gao Y.-S., Alvarez C., Nelson D.S., Sztul E. J. Biol. Chem. 273:33825-33834(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-48; 88-179 AND 223-285. Strain: Sprague-Dawley. Tissue: Liver.
[4]	"58K, a microtubule-binding Golgi protein, is a formiminotransferase cyclodeaminase." Bashour A.-M., Bloom G.S. J. Biol. Chem. 273:19612-19617(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 48-65; 115-136; 156-165; 257-268; 291-299; 307-318; 321-341 AND 394-413, SUBCELLULAR LOCATION. Tissue: Liver.
[5]	"A novel type of regulation of the vimentin intermediate filament cytoskeleton by a Golgi protein." Gao Y.S., Vrielink A., MacKenzie R., Sztul E. Eur. J. Cell Biol. 81:391-401(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer." Mao Y., Vyas N.K., Vyas M.N., Chen D.H., Ludtke S.J., Chiu W., Quiocho F.A. EMBO J. 23:2963-2971(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.42 ANGSTROMS), SUBUNIT, ACTIVE SITE FOR CYCLODEAMINASE ACTIVITY.
[7]	"Normal mode refinement of anisotropic thermal parameters for a supramolecular complex at 3.42-A crystallographic resolution." Poon B.K., Chen X., Lu M., Vyas N.K., Quiocho F.A., Wang Q., Ma J. Proc. Natl. Acad. Sci. U.S.A. 104:7869-7874(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.42 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF079233 mRNA. Translation: AAC28849.3.
BC091134 mRNA. Translation: AAH91134.1.

IPI

IPI00211392.

RefSeq

NP_446019.1. NM_053567.1.

UniGene

Rn.20140.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TT9	X-ray	3.42	A/B/C/D	1-541	[»]
2PFD	X-ray	3.42	A/B/C/D	1-541	[»]

ProteinModelPortal

O88618.

SMR

O88618. Positions 2-541.

ModBase

Search...

Protein-protein interaction databases

STRING

10116.ENSRNOP00000001699.

PTM databases

PhosphoSite

O88618.

Proteomic databases

PaxDb

O88618.

PRIDE

O88618.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000001699; ENSRNOP00000001699; ENSRNOG00000001261.

GeneID

89833.

KEGG

rno:89833.

UCSC

RGD:70915. rat.

Organism-specific databases

CTD

10841.

RGD

70915. Ftcd.

Phylogenomic databases

eggNOG

COG3404.

GeneTree

ENSGT00390000005581.

HOGENOM

HOG000006949.

HOVERGEN

HBG000168.

InParanoid

O88618.

KO

K13990.

OMA

TVASLWP.

OrthoDB

EOG4FTW0C.

Enzyme and pathway databases

UniPathway

UPA00193.
UPA00379; UER00555.

Gene expression databases

Genevestigator

O88618.

GermOnline

ENSRNOG00000001261. Rattus norvegicus.

Family and domain databases

Gene3D

3.30.70.670. 1 hit.
3.30.990.10. 1 hit.

InterPro

IPR007044. Cyclodeamin/CycHdrlase.
IPR013802. Formiminotransferase_C.
IPR004227. Formiminotransferase_cat.
IPR012886. Formiminotransferase_N.
IPR022384. FormiminoTrfase_N/C_subdom.
[Graphical view]

Pfam

PF02971. FTCD. 1 hit.
PF04961. FTCD_C. 1 hit.
PF07837. FTCD_N. 1 hit.
[Graphical view]

SUPFAM

SSF101262. Cyclodeamin/cyclohydro. 1 hit.
SSF55116. Formiminotr. 2 hits.

TIGRFAMs

TIGR02024. FtcD. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O88618.

NextBio

617760.

Entry information

Entry name

FTCD_RAT

Accession

Primary (citable) accession number: O88618
Secondary accession number(s): Q5BKB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	June 6, 2002
Last modified:	April 3, 2013
This is version 117 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program