Reviewed, UniProtKB/Swiss-Prot P15925 (FOLC_LACCA)

Names and origin

Protein names

Recommended name:
    Folylpolyglutamate synthase
    EC=6.3.2.17
Alternative name(s):
    Folylpoly-gamma-glutamate synthetase
      Short name=FPGS
    Tetrahydrofolylpolyglutamate synthase
      Short name=Tetrahydrofolate synthase

Gene names

Name:

fgs

Organism

Lactobacillus casei

Taxonomic identifier

1582 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Conversion of folates to polyglutamate derivatives. It preferes 5,10-methylenetetrahydrofolate, rather than 10-formyltetrahydrofolate as folate substrate.
Catalytic activity	ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).
Pathway	Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis.
Subunit structure	Monomer.
Sequence similarities	Belongs to the folylpolyglutamate synthase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	folic acid and derivative biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon compound metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolylpolyglutamate synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 428

428

Folylpolyglutamate synthase

PRO_0000168305

Regions

Nucleotide binding

46 – 52

7

ATP

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

428

Helix Strand Turn

Details...

Helix

3 – 10

8

Helix

23 – 31

9

Helix

35 – 37

3

Beta strand

38 – 45

8

Beta strand

47 – 49

3

Helix

50 – 63

14

Beta strand

68 – 71

4

Beta strand

76 – 78

3

Helix

79 – 82

4

Beta strand

83 – 85

3

Helix

92 – 112

21

Helix

120 – 134

15

Beta strand

138 – 143

6

Beta strand

159 – 163

5

Helix

178 – 185

8

Helix

186 – 188

3

Beta strand

195 – 197

3

Helix

202 – 215

14

Beta strand

219 – 221

3

Turn

222 – 224

3

Beta strand

225 – 233

9

Beta strand

235 – 243

9

Beta strand

248 – 255

8

Helix

261 – 279

19

Helix

285 – 293

9

Beta strand

300 – 305

6

Turn

306 – 309

4

Beta strand

310 – 313

4

Helix

318 – 331

14

Beta strand

337 – 340

4

Helix

351 – 358

8

Beta strand

360 – 364

5

Helix

391 – 401

11

Beta strand

407 – 411

5

Helix

413 – 424

12

Sequences

	Sequence		Length	Mass (Da)
	P15925-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: E4B0B9ED62140181	FASTA	428	46,589
	10 20 30 40 50 60 MNYTETVAYI HSFPRLAKTG DHRRILTLLH ALGNPQQQGR YIHVTGTNGK GSAANAIAHV 70 80 90 100 110 120 LEASGLTVGL YTSPFIMRFN ERIMIDHEPI PDAALVNAVA FVRAALERLQ QQQADFNVTE 130 140 150 160 170 180 FEFITALGYW YFRQRQVDVA VIEVGIGGDT DSTNVITPVV SVLTEVALDH QKLLGHTITA 190 200 210 220 230 240 IAKHKAGIIK RGIPVVTGNL VPDAAAVVAA KVATTGSQWL RFDRDFSVPK AKLHGWGQRF 250 260 270 280 290 300 TYEDQDGRIS DLEVPLVGDY QQRNMAIAIQ TAKVYAKQTE WPLTPQNIRQ GLAASHWPAR 310 320 330 340 350 360 LEKISDTPLI VIDGAHNPDG INGLITALKQ LFSQPITVIA GILADKDYAA MADRLTAAFS 370 380 390 400 410 420 TVYLVPVPGT PRALPEAGYE ALHEGRLKDS WQEALAASLN DVPDQPIVIT GSLYLASAVR QTLLGGKS

References

[1]	"Cloning and expression of the gene encoding Lactobacillus casei folylpoly-gamma-glutamate synthetase in Escherichia coli and determination of its primary structure." Toy J., Bognar A.L. J. Biol. Chem. 265:2492-2499(1990) [PubMed: 2105929] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Structural homologies with ATP- and folate-binding enzymes in the crystal structure of folylpolyglutamate synthetase." Sun X., Bognar A.L., Baker E.N., Smith C.A. Proc. Natl. Acad. Sci. U.S.A. 95:6647-6652(1998) [PubMed: 9618466] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J05221 Genomic DNA. Translation: AAA88210.1.

PIR

A35534.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FGS	X-ray	2.40	A	1-428	[»]
1JBV	X-ray	1.95	A	1-428	[»]
1JBW	X-ray	1.85	A	1-428	[»]
2GC5	X-ray	1.85	A	1-428	[»]
2GC6	X-ray	1.90	A	1-428	[»]
2GCA	X-ray	2.40	A	1-428	[»]
2GCB	X-ray	2.30	A	1-428	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

6.3.2.17. 610.

Family and domain databases

InterPro

IPR018109. Folylpolyglutamate_synth_CS.
IPR001645. Fpolygl_synthtse.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
[Graphical view]

Gene3D

G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.

PANTHER

PTHR11136. Fpolygl_synthtse. 1 hit.

Pfam

PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01499. folC. 1 hit.

PROSITE

PS01011. FOLYLPOLYGLU_SYNT_1. 1 hit.
PS01012. FOLYLPOLYGLU_SYNT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FOLC_LACCA

Accession

Primary (citable) accession number: P15925

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)