Q9HJA6 (RIFK_THEAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Riboflavin kinase
Short name=RFK
EC=2.7.1.161

Alternative name(s):
CTP-dependent riboflavin kinase
CTP:riboflavin 5'-phosphotransferase
Flavokinase

Gene names

Name:	ribK
Ordered Locus Names:	Ta1064

Organism

Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]

Taxonomic identifier

273075 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma › Thermoplasma acidophilum

Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the CTP-dependent phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) By similarity. HAMAP-Rule MF_01285
Catalytic activity	CTP + riboflavin = CDP + FMN. HAMAP-Rule MF_01285
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1. HAMAP-Rule MF_01285
Sequence similarities	Belongs to the archaeal riboflavin kinase family.

Ontologies

Keywords
Ligand	FMN Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	FMN biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway riboflavin biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW riboflavin kinase activity Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 220

220

Riboflavin kinase HAMAP-Rule MF_01285

PRO_0000322106

Regions

Nucleotide binding

102 – 107

6

CDP By similarity

Nucleotide binding

200 – 203

4

CDP By similarity

Region

1 – 92

92

H-T-H motif-like HAMAP-Rule MF_01285

Region

93 – 220

128

Riboflavin kinase HAMAP-Rule MF_01285

Sites

Metal binding

131

1

Magnesium By similarity

Metal binding

133

1

Magnesium By similarity

Binding site

188

1

FMN By similarity

Binding site

195

1

FMN By similarity

Secondary structure

1

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220

Helix Strand Turn

Details...

Helix

6 – 17

12

Turn

18 – 20

3

Beta strand

21 – 25

5

Helix

28 – 35

8

Helix

39 – 51

13

Beta strand

54 – 60

7

Beta strand

63 – 68

6

Helix

70 – 86

17

Beta strand

93 – 99

7

Helix

116 – 122

7

Beta strand

133 – 136

4

Helix

138 – 140

3

Helix

141 – 149

9

Beta strand

153 – 155

3

Beta strand

168 – 175

8

Beta strand

178 – 187

10

Beta strand

192 – 197

6

Beta strand

213 – 218

6

Sequences

	Sequence		Length	Mass (Da)
	Q9HJA6 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: BB0F694447629612	FASTA	220	24,997
	10 20 30 40 50 60 METDDQYYRA IKKIKEAAEA SNRAYLTSSK LADMLGISQQ SASRIIIDLE KNGYITRTVT 70 80 90 100 110 120 KRGQILNITE KGLDVLYTEF ADLSRILAIK NNVVITGTVT SGMGEGRYYV ARKQYIIQFQ 130 140 150 160 170 180 EKLGIIPYLG TLNIKVDQAS LPELRKIRGF RGIHIEGFKT EDRTFGSVKA FPAKIQNIPC 190 200 210 220 FVIMPERTVY TDVIEIISDK YLREEINLHD GDRVSVEVYT

References

[1]

"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum." Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W. Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL445066 Genomic DNA. Translation: CAC12192.1.

RefSeq

NP_394524.1. NC_002578.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CTA	X-ray	2.20	A	2-220	[»]

ProteinModelPortal

Q9HJA6.

SMR

Q9HJA6. Positions 5-220.

ModBase

Search...

Protein-protein interaction databases

STRING

273075.Ta1064.

Proteomic databases

PRIDE

Q9HJA6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAC12192; CAC12192; CAC12192.

GeneID

1456578.

KEGG

tac:Ta1064.

Phylogenomic databases

eggNOG

COG1339.

HOGENOM

HOG000015512.

KO

K07732.

OMA

GAYYVRQ.

ProtClustDB

PRK14165.

Enzyme and pathway databases

UniPathway

UPA00276; UER00929.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.
2.40.30.30. 1 hit.

HAMAP

MF_01285. Riboflavin_kinase. Fused.

InterPro

IPR023602. Riboflavin_kinase_CTP-dep.
IPR023465. Riboflavin_kinase_domain.
IPR000835. Tscrpt_reg_HTH_MarR-typ.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF01982. CTP-dep_RFKase. 1 hit.
PF01047. MarR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9HJA6.

Entry information

Entry name

RIFK_THEAC

Accession

Primary (citable) accession number: Q9HJA6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program