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Protein

Nitric oxide reductase

Gene

fprA

Organism
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has nitric oxide reductase activity in combination with Hrb; probably involved in nitrosative stress protection.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi81Iron 1By similarity1
Metal bindingi83Iron 1By similarity1
Metal bindingi85Iron 2By similarity1
Metal bindingi148Iron 1By similarity1
Metal bindingi167Iron 1By similarity1
Metal bindingi167Iron 2By similarity1
Metal bindingi228Iron 2By similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Flavoprotein, FMN, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nitric oxide reductase (EC:1.-.-.-)
Alternative name(s):
FMN protein FprA
Flavoprotein A
Type A flavoprotein FprA
Gene namesi
Name:fprA
Ordered Locus Names:Moth_1287
OrganismiMoorella thermoacetica (strain ATCC 39073 / JCM 9320)
Taxonomic identifieri264732 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella
Proteomesi
  • UP000007053 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002168051 – 399Nitric oxide reductaseAdd BLAST399

Expressioni

Inductioni

Constitutively expressed.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi264732.Moth_1287.

Structurei

Secondary structure

1399
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Beta strandi11 – 13Combined sources3
Beta strandi16 – 20Combined sources5
Turni25 – 28Combined sources4
Beta strandi35 – 37Combined sources3
Beta strandi40 – 42Combined sources3
Beta strandi44 – 46Combined sources3
Beta strandi48 – 50Combined sources3
Helixi55 – 57Combined sources3
Helixi58 – 68Combined sources11
Beta strandi75 – 78Combined sources4
Helixi84 – 87Combined sources4
Helixi90 – 96Combined sources7
Beta strandi101 – 104Combined sources4
Helixi106 – 115Combined sources10
Beta strandi122 – 125Combined sources4
Beta strandi131 – 133Combined sources3
Beta strandi138 – 143Combined sources6
Beta strandi147 – 149Combined sources3
Beta strandi153 – 157Combined sources5
Turni158 – 161Combined sources4
Beta strandi162 – 166Combined sources5
Turni167 – 169Combined sources3
Helixi180 – 182Combined sources3
Helixi185 – 199Combined sources15
Helixi201 – 203Combined sources3
Helixi204 – 216Combined sources13
Beta strandi222 – 229Combined sources8
Helixi236 – 248Combined sources13
Beta strandi253 – 259Combined sources7
Beta strandi262 – 264Combined sources3
Helixi265 – 279Combined sources15
Beta strandi283 – 288Combined sources6
Helixi289 – 291Combined sources3
Helixi294 – 303Combined sources10
Beta strandi305 – 310Combined sources6
Helixi320 – 322Combined sources3
Helixi323 – 332Combined sources10
Beta strandi338 – 348Combined sources11
Helixi351 – 361Combined sources11
Beta strandi365 – 367Combined sources3
Beta strandi373 – 377Combined sources5
Helixi380 – 397Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YCFX-ray3.00A/B/C/D2-399[»]
1YCGX-ray2.80A/B/C/D2-399[»]
1YCHX-ray2.80A/B/C/D2-399[»]
ProteinModelPortaliQ9FDN7.
SMRiQ9FDN7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9FDN7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini255 – 394Flavodoxin-likePROSITE-ProRule annotationAdd BLAST140

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 221Zinc metallo-hydrolaseAdd BLAST190

Sequence similaritiesi

In the N-terminal section; belongs to the zinc metallo-hydrolase group 3 family.Curated
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CNW. Bacteria.
COG0426. LUCA.
HOGENOMiHOG000224528.
OMAiIYCTEIA.
OrthoDBiPOG091H01XB.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
3.60.15.10. 1 hit.
InterProiIPR008254. Flavodoxin/NO_synth.
IPR029039. Flavoprotein-like_dom.
IPR001279. Metallo-B-lactamas.
IPR016440. Rubredoxin-O_OxRdtase.
[Graphical view]
PfamiPF00258. Flavodoxin_1. 1 hit.
PF00753. Lactamase_B. 1 hit.
[Graphical view]
PIRSFiPIRSF005243. ROO. 1 hit.
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF56281. SSF56281. 1 hit.
PROSITEiPS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9FDN7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQPVAITDG IYWVGAVDWN IRYFHGPAFS THRGTTYNAY LIVDDKTALV
60 70 80 90 100
DTVYEPFKEE LIAKLKQIKD PVKLDYLVVN HTESDHAGAF PAIMELCPDA
110 120 130 140 150
HVLCTQRAFD SLKAHYSHID FNYTIVKTGT SVSLGKRSLT FIEAPMLHWP
160 170 180 190 200
DSMFTYVPEE ALLLPNDAFG QHIATSVRFD DQVDAGLIMD EAAKYYANIL
210 220 230 240 250
MPFSNLITKK LDEIQKINLA IKTIAPSHGI IWRKDPGRII EAYARWAEGQ
260 270 280 290 300
GKAKAVIAYD TMWLSTEKMA HALMDGLVAG GCEVKLFKLS VSDRNDVIKE
310 320 330 340 350
ILDARAVLVG SPTINNDILP VVSPLLDDLV GLRPKNKVGL AFGAYGWGGG
360 370 380 390
AQKILEERLK AAKIELIAEP GPTVQWVPRG EDLQRCYELG RKIAARIAD
Length:399
Mass (Da):44,297
Last modified:March 1, 2001 - v1
Checksum:i198C380C41C58614
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF202316 Genomic DNA. Translation: AAG00802.1.
CP000232 Genomic DNA. Translation: ABC19601.1.
RefSeqiWP_011392801.1. NC_007644.1.
YP_430144.1. NC_007644.1.

Genome annotation databases

EnsemblBacteriaiABC19601; ABC19601; Moth_1287.
GeneIDi3831550.
KEGGimta:Moth_1287.
PATRICi22639806. VBIMooThe6753_1381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF202316 Genomic DNA. Translation: AAG00802.1.
CP000232 Genomic DNA. Translation: ABC19601.1.
RefSeqiWP_011392801.1. NC_007644.1.
YP_430144.1. NC_007644.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YCFX-ray3.00A/B/C/D2-399[»]
1YCGX-ray2.80A/B/C/D2-399[»]
1YCHX-ray2.80A/B/C/D2-399[»]
ProteinModelPortaliQ9FDN7.
SMRiQ9FDN7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi264732.Moth_1287.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC19601; ABC19601; Moth_1287.
GeneIDi3831550.
KEGGimta:Moth_1287.
PATRICi22639806. VBIMooThe6753_1381.

Phylogenomic databases

eggNOGiENOG4105CNW. Bacteria.
COG0426. LUCA.
HOGENOMiHOG000224528.
OMAiIYCTEIA.
OrthoDBiPOG091H01XB.

Miscellaneous databases

EvolutionaryTraceiQ9FDN7.

Family and domain databases

Gene3Di3.40.50.360. 1 hit.
3.60.15.10. 1 hit.
InterProiIPR008254. Flavodoxin/NO_synth.
IPR029039. Flavoprotein-like_dom.
IPR001279. Metallo-B-lactamas.
IPR016440. Rubredoxin-O_OxRdtase.
[Graphical view]
PfamiPF00258. Flavodoxin_1. 1 hit.
PF00753. Lactamase_B. 1 hit.
[Graphical view]
PIRSFiPIRSF005243. ROO. 1 hit.
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF56281. SSF56281. 1 hit.
PROSITEiPS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFPRA_MOOTA
AccessioniPrimary (citable) accession number: Q9FDN7
Secondary accession number(s): Q2RIY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.