P0AC16 (FOLB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydroneopterin aldolase
Short name=DHNA
EC=4.1.2.25

Gene names

Name:	folB
Synonyms:	ygiG
Ordered Locus Names:	b3058, JW3030

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	122 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin at appreciable velocity.
Catalytic activity	2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Subunit structure	Homooctamer.
Sequence similarities	Belongs to the DHNA family.
Sequence caution	The sequence AAA89138.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Folate biosynthesis
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	dihydroneopterin aldolase activity Inferred from direct assay Ref.4. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 122

122

Dihydroneopterin aldolase

PRO_0000168269

Experimental info

Sequence conflict

81 – 82

2

EL → DV in L12966. Ref.1

Sequence conflict

100 – 122

23

GAVAR…LKENN → ASGAGGECWRNH in L12966. Ref.1

Secondary structure

1

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122

Helix Strand Turn

Details...

Beta strand

2 – 15

14

Helix

19 – 23

5

Beta strand

26 – 36

11

Helix

39 – 44

6

Helix

47 – 49

3

Helix

53 – 64

12

Beta strand

68 – 70

3

Helix

72 – 86

15

Beta strand

92 – 97

6

Beta strand

109 – 114

6

Sequences

	Sequence		Length	Mass (Da)
	P0AC16 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: BEA82C1E0AA38A55	FASTA	122	13,620
	10 20 30 40 50 60 MDIVFIEQLS VITTIGVYDW EQTIEQKLVF DIEMAWDNRK AAKSDDVADC LSYADIAETV 70 80 90 100 110 120 VSHVEGARFA LVERVAEEVA ELLLARFNSP WVRIKLSKPG AVARAANVGV IIERGNNLKE NN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Amplification of the bacA gene confers bacitracin resistance to Escherichia coli." Cain B.D., Norton P.J., Eubanks W., Nick H.S., Allen C.M. J. Bacteriol. 175:3784-3789(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / ATCC 35607 / JM83.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase." Haussmann C., Rohdich F., Schmidt E., Bacher A., Richter G. J. Biol. Chem. 273:17418-17424(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L12966 Genomic DNA. No translation available.
U28379 Genomic DNA. Translation: AAA89138.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76094.2.
AP009048 Genomic DNA. Translation: BAE77109.1.

PIR

H65093.

RefSeq

NP_417530.2. NC_000913.2.
YP_491250.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2O90	X-ray	1.07	A	1-122	[»]

ProteinModelPortal

P0AC16.

SMR

P0AC16. Positions 1-115.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36044N.

IntAct

P0AC16. 2 interactions.

STRING

511145.b3058.

Proteomic databases

PaxDb

P0AC16.

PRIDE

P0AC16.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76094; AAC76094; b3058.
BAE77109; BAE77109; BAE77109.

GeneID

12930262.
947544.

KEGG

ecj:Y75_p2984.
eco:b3058.

PATRIC

32121528. VBIEscCol129921_3151.

Organism-specific databases

EchoBASE

EB1624.

EcoGene

EG11673. folB.

Phylogenomic databases

eggNOG

COG1539.

HOGENOM

HOG000217627.

KO

K01633.

OMA

LITEKPI.

ProtClustDB

PRK11593.

Enzyme and pathway databases

BioCyc

EcoCyc:H2NEOPTERINALDOL-MONOMER.
ECOL316407:JW3030-MONOMER.
MetaCyc:H2NEOPTERINALDOL-MONOMER.

UniPathway

UPA00077; UER00154.

Gene expression databases

Genevestigator

P0AC16.

Family and domain databases

InterPro

IPR006156. Dihydroneopterin_aldolase.
IPR006157. FolB_dom.
[Graphical view]

Pfam

PF02152. FolB. 1 hit.
[Graphical view]

SMART

SM00905. FolB. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00525. folB. 1 hit.
TIGR00526. folB_dom. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0AC16.

Entry information

Entry name

FOLB_ECOLI

Accession

Primary (citable) accession number: P0AC16
Secondary accession number(s): P31055, P76659, Q2M9E7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program