O06553 (Y1155_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative pyridoxine/pyridoxamine 5'-phosphate oxidase
EC=1.4.3.5

Alternative name(s):
PNP/PMP oxidase
Short name=PNPOx
Pyridoxal 5'-phosphate synthase

Gene names

Ordered Locus Names:

Rv1155

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) Potential.
Catalytic activity	Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2. Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2.
Subunit structure	Homodimer. Ref.2 Ref.3

Ontologies

Keywords
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pyridoxal phosphate biosynthetic process Inferred from electronic annotation. Source: GOC vitamin B6 metabolic process Inferred from direct assay Ref.2. Source: MTBBASE
Molecular_function	FMN binding Inferred from direct assay Ref.2. Source: MTBBASE pyridoxal phosphate binding Inferred from direct assay Ref.2. Source: MTBBASE pyridoxamine-phosphate oxidase 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 – 147

147

Putative pyridoxine/pyridoxamine 5'-phosphate oxidase

PRO_0000399901

Regions

Region

32 – 35

4

FMN binding

Region

34 – 35

2

Pyridoxal phosphate binding

Region

55 – 57

3

FMN binding

Region

55 – 57

3

Pyridoxal phosphate binding

Sites

Binding site

37

1

FMN

Binding site

50

1

FMN; via carbonyl oxygen

Binding site

79

1

Pyridoxal phosphate

Secondary structure

1

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147

Helix Strand Turn

Details...

Helix

6 – 15

10

Beta strand

18 – 25

8

Beta strand

31 – 37

7

Beta strand

39 – 41

3

Turn

42 – 45

4

Beta strand

46 – 52

7

Helix

56 – 63

8

Beta strand

66 – 72

7

Beta strand

74 – 77

4

Beta strand

79 – 85

7

Helix

98 – 110

13

Helix

117 – 126

10

Beta strand

129 – 135

7

Beta strand

138 – 142

5

Sequences

	Sequence		Length	Mass (Da)
	O06553 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: DAF63639A04D6A0D	FASTA	147	16,301
	10 20 30 40 50 60 MARQVFDDKL LAVISGNSIG VLATIKHDGR PQLSNVQYHF DPRKLLIQVS IAEPRAKTRN 70 80 90 100 110 120 LRRDPRASIL VDADDGWSYA VAEGTAQLTP PAAAPDDDTV EALIALYRNI AGEHSDWDDY 130 140 RQAMVTDRRV LLTLPISHVY GLPPGMR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Structures of Mycobacterium tuberculosispyridoxine 5'-phosphate oxidase and its complexes with flavin mononucleotide and pyridoxal 5'-phosphate." Biswal B.K., Cherney M.M., Wang M., Garen C., James M.N. Acta Crystallogr. D 61:1492-1499(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH FMN AND PYRIDOXAL PHOSPHATE, SUBUNIT.
[3]	"Crystal structure of the conserved hypothetical protein Rv1155 from Mycobacterium tuberculosis." Canaan S., Sulzenbacher G., Roig-Zamboni V., Scappuccini-Calvo L., Frassinetti F., Maurin D., Cambillau C., Bourne Y. FEBS Lett. 579:215-221(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842575 Genomic DNA. Translation: CAB09014.1.
AL123456 Genomic DNA. Translation: CCP43910.1.

PIR

D70555.

RefSeq

NP_215671.1. NC_000962.3.
YP_006514527.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W9A	X-ray	1.80	A/B	1-147	[»]
1XXO	X-ray	1.80	A/B	1-147	[»]
1Y30	X-ray	2.20	A/B	1-147	[»]
2AQ6	X-ray	1.70	A/B	1-147	[»]

ProteinModelPortal

O06553.

SMR

O06553. Positions 5-147.

ModBase

Search...

Protein-protein interaction databases

STRING

83332.Rv1155.

Proteomic databases

PRIDE

O06553.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

13319731.
885604.

KEGG

mtu:Rv1155.
mtv:RVBD_1155.

PATRIC

18151117. VBIMycTub87468_1296.

Organism-specific databases

TubercuList

Rv1155.

Phylogenomic databases

eggNOG

NOG07001.

HOGENOM

HOG000022434.

KO

K07005.

OMA

DRAKTRN.

ProtClustDB

CLSK790983.

Family and domain databases

Gene3D

2.30.110.10. 1 hit.

InterPro

IPR019920. F420-binding_dom_put.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]

Pfam

PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]

SUPFAM

SSF50475. FMN_binding. 1 hit.

TIGRFAMs

TIGR03618. Rv1155_F420. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O06553.

Entry information

Entry name

Y1155_MYCTU

Accession

Primary (citable) accession number: O06553
Secondary accession number(s): L0T7G6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2010
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program