P71278 (P71278_ENTCL) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Pentaerythritol tetranitrate reductase EMBL AAB38683.1

Gene names

Name:

onr EMBL AAB38683.1

Organism

Enterobacter cloacae EMBL AAB38683.1

Taxonomic identifier

550 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter › Enterobacter cloacae complex

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	FMN PDB 1GVQ PDB 1GVR PDB 1GVS PDB 1H50 PDB 1H51 PDB 1H60 PDB 1H62 PDB 1H63 PDB 1VYP PDB 1VYS PDB 1H61 PDB 1GVO PDB 1VYR PDB 2ABA PDB 2ABB PDB 3F03 PDB 3KFT PDB 3P62 PDB 3P67 Flavoprotein PDB 1GVQ PDB 1GVR PDB 1GVS PDB 1H50 PDB 1H51 PDB 1H60 PDB 1H62 PDB 1H63 PDB 1VYP PDB 1VYS PDB 1H61 PDB 1GVO PDB 1VYR PDB 2ABA PDB 2ABB PDB 3F03 PDB 3KFT PDB 3P62 PDB 3P67 NAD PDB 3KFT Nucleotide-binding PDB 1GVQ PDB 1GVR PDB 1GVS PDB 1H50 PDB 1H51 PDB 1H60 PDB 1H62 PDB 1H63 PDB 1VYP PDB 1VYS PDB 1H61 PDB 1GVO PDB 1VYR PDB 2ABA PDB 2ABB PDB 3F03 PDB 3KFT PDB 3P62 PDB 3P67
Technical term	3D-structure PDB 1GVQ PDB 1GVR PDB 1GVS PDB 1H50 PDB 1H51 PDB 1H60 PDB 1H62 PDB 1H63 PDB 1VYP PDB 1VYS PDB 1H61 PDB 1GVO PDB 1VYR PDB 2ABA PDB 2ABB PDB 3F03 PDB 3KFT PDB 3P62 PDB 3P67 PDB 3P74 PDB 3P7Y PDB 3P82 PDB 3P81 PDB 3P80 PDB 3P84 PDB 3P8I PDB 3P8J
Gene Ontology (GO)
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Nucleotide binding	25 – 27	3	FMN{EI1,EI10,EI12,EI13,EI14,EI15,EI16, EI17,EI18,EI19,EI2,EI20,EI3,EI4,EI5,EI6,EI7,EI8,EI9}
	Nucleotide binding	182 – 185	4	NAD PDB 3KFT
	Nucleotide binding	302 – 303	2	FMN{EI1,EI10,EI12,EI13,EI14,EI15,EI16, EI17,EI18,EI19,EI2,EI20,EI3,EI4,EI5,EI6,EI7,EI8,EI9}
	Nucleotide binding	324 – 325	2	FMN{EI1,EI10,EI12,EI13,EI14,EI15,EI16, EI17,EI18,EI19,EI2,EI20,EI3,EI4,EI5,EI6,EI7,EI8,EI9}
	Region	182 – 185	4	Progesterone binding PDB 1H60 PDB 2ABA
Sites
	Binding site	27	1	NAD PDB 3KFT
	Binding site	59	1	FMN; via amide nitrogen{EI1,EI10,EI13, EI14,EI15,EI16,EI17,EI18,EI19,EI2,EI20,EI3,EI4,EI5,EI6,EI7,EI8,EI9}
	Binding site	69	1	NAD PDB 3KFT
	Binding site	69	1	Progesterone PDB 1H60 PDB 2ABA
	Binding site	101	1	FMN{EI1,EI10,EI12,EI13,EI14,EI15,EI16, EI17,EI18,EI19,EI2,EI20,EI3,EI4,EI5,EI6,EI7,EI8,EI9}
	Binding site	143	1	Progesterone PDB 2ABA
	Binding site	182	1	FMN{EI1,EI10,EI12,EI13,EI14,EI15,EI16, EI17,EI18,EI19,EI2,EI20,EI3,EI4,EI5,EI6,EI7,EI8,EI9}
	Binding site	234	1	FMN{EI1,EI10,EI12,EI13,EI14,EI15,EI16, EI17,EI18,EI19,EI2,EI20,EI3,EI4,EI5,EI6,EI7,EI8,EI9}
	Binding site	325	1	NAD PDB 3KFT
	Binding site	352	1	FMN PDB 1GVQ PDB 1H50 PDB 1H63 PDB 2ABB

Sequences

	Sequence		Length	Mass (Da)
	P71278 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 2B34CB1E960AC648	FASTA	365	39,489
	10 20 30 40 50 60 MSAEKLFTPL KVGAVTAPNR VFMAPLTRLR SIEPGDIPTP LMGEYYRQRA SAGLIISEAT 70 80 90 100 110 120 QISAQAKGYA GAPGLHSPEQ IAAWKKITAG VHAEDGRIAV QLWHTGRISH SSIQPGGQAP 130 140 150 160 170 180 VSASALNANT RTSLRDENGN AIRVDTTTPR ALELDEIPGI VNDFRQAVAN AREAGFDLVE 190 200 210 220 230 240 LHSAHGYLLH QFLSPSSNQR TDQYGGSVEN RARLVLEVVD AVCNEWSADR IGIRVSPIGT 250 260 270 280 290 300 FQNVDNGPNE EADALYLIEE LAKRGIAYLH MSETDLAGGK PYSEAFRQKV RERFHGVIIG 310 320 330 340 350 360 AGAYTAEKAE DLIGKGLIDA VAFGRDYIAN PDLVARLQKK AELNPQRPES FYGGGAEGYT DYPSL

References

[1]	"Degradation of pentaerythritol tetranitrate by Enterobacter cloacae PB2." Binks P.R., French C.E., Nicklin S., Bruce N.C. Appl. Environ. Microbiol. 62:1214-1219(1996) [PubMed: 8919782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: PB2 EMBL AAB38683.1.
[2]	"Sequence and properties of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2." French C.E., Nicklin S., Bruce N.C. J. Bacteriol. 178:6623-6627(1996) [PubMed: 8932320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: PB2 EMBL AAB38683.1.
[3]	"Crystal structure of pentaerythritol tetranitrate reductase: "flipped" binding geometries for steroid substrates in different redox states of the enzyme." Barna T.M., Khan H., Bruce N.C., Barsukov I., Scrutton N.S., Moody P.C. J. Mol. Biol. 310:433-447(2001) [PubMed: 11428899] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 2-365 IN COMPLEX WITH FMN AND PROGESTERONE.
[4]	"Kinetic and structural basis of reactivity of pentaerythritol tetranitrate reductase with NADPH, 2-cyclohexenone, nitroesters, and nitroaromatic explosives." Khan H., Harris R.J., Barna T., Craig D.H., Bruce N.C., Munro A.W., Moody P.C., Scrutton N.S. J. Biol. Chem. 277:21906-21912(2002) [PubMed: 11923299] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 2-365 IN COMPLEX WITH FMN.
[5]	"Atomic resolution structures and solution behavior of enzyme-substrate complexes of Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase. Multiple conformational states and implications for the mechanism of nitroaromatic explosive degradation." Khan H., Barna T., Harris R.J., Bruce N.C., Barsukov I., Munro A.W., Moody P.C., Scrutton N.S. J. Biol. Chem. 279:30563-30572(2004) [PubMed: 15128738] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.90 ANGSTROMS) OF 2-365 IN COMPLEX WITH FMN.
[6]	"Structure-based insight into the asymmetric bioreduction of the C=C double bond of alpha,beta-unsaturated nitroalkenes by pentaerythritol tetranitrate reductase." Toogood H.S., Fryszkowska A., Hare V., Fisher K., Roujeinikova A., Leys D., Gardiner J.M., Stephens G.M., Scrutton N.S. Submitted (OCT-2008) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.34 ANGSTROMS) OF 2-365 IN COMPLEX WITH FMN.
[7]	"Proton transfer in the oxidative half-reaction of pentaerythritol tetranitrate reductase. Structure of the reduced enzyme-progesterone complex and the roles of residues Tyr186, His181, His184." Khan H., Barna T., Bruce N.C., Munro A.W., Leys D., Scrutton N.S. FEBS J. 272:4660-4671(2005) [PubMed: 16156787] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.00 ANGSTROMS) OF 2-365 IN COMPLEX WITH FMN AND PROGESTERONE.
[8]	"Evidence to support the hypothesis that promoting vibrations enhance the rate of an enzyme catalyzed H-tunneling reaction." Pudney C.R., Hay S., Levy C., Pang J., Sutcliffe M.J., Leys D., Scrutton N.S. J. Am. Chem. Soc. 131:17072-17073(2009) [PubMed: 19891489] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-365 IN COMPLEX WITH FMN AND NAD.
[9]	"A Site-Saturated Mutagenesis Study of Pentaerythritol Tetranitrate Reductase Reveals that Residues 181 and 184 Influence Ligand Binding, Stereochemistry and Reactivity." Toogood H.S., Fryszkowska A., Hulley M., Sakuma M., Mansell D., Stephens G.M., Gardiner J.M., Scrutton N.S. Chembiochem 12:738-749(2011) [PubMed: 21374779] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS).
[10]	"Focused directed evolution of pentaerythritol tetranitrate reductase by using automated anaerobic kinetic screening of site-saturated libraries." Hulley M.E., Toogood H.S., Fryszkowska A., Mansell D., Stephens G.M., Gardiner J.M., Scrutton N.S. Chembiochem 11:2433-2447(2010) [PubMed: 21064170] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH FMN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U68759 Genomic DNA. Translation: AAB38683.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GVO	X-ray	1.38	A	2-365	[»]
1GVQ	X-ray	2.00	A	2-365	[»]
1GVR	X-ray	1.38	A	2-365	[»]
1GVS	X-ray	1.38	A	2-365	[»]
1H50	X-ray	1.50	A	2-365	[»]
1H51	X-ray	1.60	A	2-365	[»]
1H60	X-ray	1.60	A	2-365	[»]
1H61	X-ray	1.40	A	2-365	[»]
1H62	X-ray	1.90	A	2-365	[»]
1H63	X-ray	1.62	A	2-365	[»]
1VYP	X-ray	1.27	X	2-365	[»]
1VYR	X-ray	0.90	A	2-365	[»]
1VYS	X-ray	1.80	X	2-365	[»]
2ABA	X-ray	1.05	A	2-365	[»]
2ABB	X-ray	1.00	A	2-365	[»]
3F03	X-ray	1.34	K	2-365	[»]
3KFT	X-ray	2.10	A/B	2-365	[»]
3P62	X-ray	1.40	A	1-365	[»]
3P67	X-ray	1.50	A	1-365	[»]
3P74	X-ray	1.20	A	1-365	[»]
3P7Y	X-ray	1.20	A	1-365	[»]
3P80	X-ray	1.20	A	1-365	[»]
3P81	X-ray	1.20	A	1-365	[»]
3P82	X-ray	2.20	A	1-365	[»]
3P84	X-ray	1.10	A	1-365	[»]
3P8I	X-ray	1.19	A	1-365	[»]
3P8J	X-ray	1.00	A	1-365	[»]

ProteinModelPortal

P71278.

SMR

P71278. Positions 2-365.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

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Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR001155. OxRdtase_FMN_N.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF00724. Oxidored_FMN. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

P71278_ENTCL

Accession

Primary (citable) accession number: P71278

Entry history

Integrated into UniProtKB/TrEMBL:	February 1, 1997
Last sequence update:	February 1, 1997
Last modified:	July 27, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)