P23295 (NOR_FUSOX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome P450 55A1
EC=1.14.-.-

Alternative name(s):
CYPLVA1
Cytochrome P450 DNIR
Cytochrome P450nor
Nitric oxide reductase

Gene names

Name:	CYP55A1
Synonyms:	CYP55

Organism

Fusarium oxysporum (Panama disease fungus)

Taxonomic identifier

5507 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › mitosporic Hypocreales › Fusarium › Fusarium oxysporum species complex

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in a dissimilatory reduction of nitrite, acts as a nitric oxide reductase.
Cofactor	Heme group.
Induction	By nitrate/nitrite.
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 403

402

Cytochrome P450 55A1

PRO_0000052039

Sites

Metal binding

352

1

Iron (heme axial ligand)

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.3

Secondary structure

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403

Helix Strand Turn

Details...

Beta strand

7 – 9

3

Helix

21 – 28

8

Beta strand

30 – 35

6

Beta strand

41 – 45

5

Helix

48 – 56

9

Helix

74 – 79

6

Helix

86 – 88

3

Helix

93 – 101

9

Helix

102 – 105

4

Helix

107 – 131

25

Helix

140 – 143

4

Turn

144 – 146

3

Helix

147 – 157

11

Helix

161 – 163

3

Helix

164 – 175

12

Helix

181 – 204

24

Helix

210 – 217

8

Turn

218 – 222

5

Helix

226 – 257

32

Helix

259 – 267

9

Helix

269 – 271

3

Helix

272 – 282

11

Beta strand

291 – 296

6

Beta strand

298 – 300

3

Beta strand

303 – 305

3

Beta strand

310 – 313

4

Helix

315 – 318

4

Turn

322 – 324

3

Beta strand

325 – 327

3

Helix

348 – 350

3

Helix

355 – 372

18

Beta strand

377 – 380

4

Helix

382 – 384

3

Beta strand

396 – 398

3

Beta strand

400 – 402

3

Sequences

	Sequence		Length	Mass (Da)
	P23295 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 7FDD97D8E0FB9215	FASTA	403	44,372
	10 20 30 40 50 60 MASGAPSFPF SRASGPEPPA EFAKLRATNP VSQVKLFDGS LAWLVTKHKD VCFVATSEKL 70 80 90 100 110 120 SKVRTRQGFP ELSASGKQAA KAKPTFVDMD PPEHMHQRSM VEPTFTPEAV KNLQPYIQRT 130 140 150 160 170 180 VDDLLEQMKQ KGCANGPVDL VKEFALPVPS YIIYTLLGVP FNDLEYLTQQ NAIRTNGSST 190 200 210 220 230 240 AREASAANQE LLDYLAILVE QRLVEPKDDI ISKLCTEQVK PGNIDKSDAV QIAFLLLVAG 250 260 270 280 290 300 NATMVNMIAL GVATLAQHPD QLAQLKANPS LAPQFVEELC RYHTASALAI KRTAKEDVMI 310 320 330 340 350 360 GDKLVRANEG IIASNQSANR DEEVFENPDE FNMNRKWPPQ DPLGFGFGDH RCIAEHLAKA 370 380 390 400 ELTTVFSTLY QKFPDLKVAV PLGKINYTPL NRDVGIVDLP VIF

References

[1]	"Nucleotide sequence of the unique nitrate/nitrite-inducible cytochrome P-450 cDNA from Fusarium oxysporum." Kizawa H., Tomura D., Oda M., Fukamizu A., Hoshino T., Gotoh O., Yasui T., Shoun H. J. Biol. Chem. 266:10632-10637(1991) [PubMed: 2037602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: MT-811.
[2]	"Nitric oxide reductase cytochrome P-450 gene, CYP 55, of the fungus Fusarium oxysporum containing a potential binding-site for FNR, the transcription factor involved in the regulation of anaerobic growth of Escherichia coli." Tomura D., Obika K., Fukamizu A., Shoun H. J. Biochem. 116:88-94(1994) [PubMed: 7798191] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MT-811.
[3]	"N-terminal processing and amino acid sequence of two isoforms of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum." Nakahara K., Shoun H. J. Biochem. 120:1082-1087(1996) [PubMed: 9010754] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2.
[4]	"Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum." Park S.-Y., Shimizu H., Adachi S., Nakagawa A., Tanaka I., Nakahara K., Shoun H., Obayashi E., Nakamura H., Iizuka T., Shiro Y. Nat. Struct. Biol. 4:827-832(1997) [PubMed: 9334748] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]	"Proton delivery in NO reduction by fungal nitric-oxide reductase. Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes." Shimizu H., Obayashi E., Gomi Y., Arakawa H., Park S.-Y., Nakamura H., Adachi S., Shoun H., Shiro Y. J. Biol. Chem. 275:4816-4826(2000) [PubMed: 10671516] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[6]	"Structural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam." Lee D.-S., Park S.-Y., Yamane K., Obayashi E., Hori H., Shiro Y. Biochemistry 40:2669-2677(2001) [PubMed: 11258878] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[7]	"X-ray structure of nitric oxide reductase (cytochrome P450nor) at atomic resolution." Shimizu H., Park S.-Y., Shiro Y., Adachi S. Acta Crystallogr. D 58:81-89(2002) [PubMed: 11752781] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M63340 mRNA. Translation: AAA33337.1.
D14517 Genomic DNA. Translation: BAA03390.1.

PIR

JC5150.
JC5151.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CL6	X-ray	1.70	A	2-403	[»]
1CMJ	X-ray	1.70	A	2-403	[»]
1CMN	X-ray	1.70	A	2-403	[»]
1EHE	X-ray	1.70	A	2-402	[»]
1EHF	X-ray	1.70	A	2-402	[»]
1EHG	X-ray	1.70	A	2-402	[»]
1F24	X-ray	1.40	A	2-402	[»]
1F25	X-ray	1.40	A	2-402	[»]
1F26	X-ray	1.40	A	2-402	[»]
1GED	X-ray	2.00	A	1-403	[»]
1GEI	X-ray	1.60	A	1-403	[»]
1GEJ	X-ray	1.50	A	1-403	[»]
1JFB	X-ray	1.00	A	1-403	[»]
1JFC	X-ray	1.05	A	1-403	[»]
1ROM	X-ray	2.00	A	1-403	[»]
1ULW	X-ray	2.00	A	2-402	[»]
1XQD	X-ray	1.80	A	1-403	[»]
2ROM	X-ray	2.00	A	1-403	[»]

ProteinModelPortal

P23295.

SMR

P23295. Positions 5-403.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-16203.

Family and domain databases

InterPro

IPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view]

Gene3D

G3DSA:1.10.630.10. Cyt_P450. 1 hit.

Pfam

PF00067. p450. 2 hits.
[Graphical view]

PRINTS

PR00359. BP450.

SUPFAM

SSF48264. Cytochrome_P450. 1 hit.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

NOR_FUSOX

Accession

Primary (citable) accession number: P23295

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	January 23, 2007
Last modified:	September 21, 2011
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program