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Protein

Nitric oxide reductase

Gene

fprA

Organism
Moorella thermoacetica (strain ATCC 39073)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi81 – 811Iron 1By similarity
Metal bindingi83 – 831Iron 1By similarity
Metal bindingi85 – 851Iron 2By similarity
Metal bindingi148 – 1481Iron 1By similarity
Metal bindingi167 – 1671Iron 1By similarity
Metal bindingi167 – 1671Iron 2By similarity
Metal bindingi228 – 2281Iron 2By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Flavoprotein, FMN, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMTHE264732:GH0A-1341-MONOMER.

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)
Taxonomic identifieri264732 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella
Proteomesi
  • UP000007053 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 399399Nitric oxide reductasePRO_0000216805Add
BLAST

Expressioni

Inductioni

Constitutively expressed.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi264732.Moth_1287.

Structurei

Secondary structure

1
399
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Beta strandi11 – 133Combined sources
Beta strandi16 – 205Combined sources
Turni25 – 284Combined sources
Beta strandi35 – 373Combined sources
Beta strandi40 – 423Combined sources
Beta strandi44 – 463Combined sources
Beta strandi48 – 503Combined sources
Helixi55 – 573Combined sources
Helixi58 – 6811Combined sources
Beta strandi75 – 784Combined sources
Helixi84 – 874Combined sources
Helixi90 – 967Combined sources
Beta strandi101 – 1044Combined sources
Helixi106 – 11510Combined sources
Beta strandi122 – 1254Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi138 – 1436Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi153 – 1575Combined sources
Turni158 – 1614Combined sources
Beta strandi162 – 1665Combined sources
Turni167 – 1693Combined sources
Helixi180 – 1823Combined sources
Helixi185 – 19915Combined sources
Helixi201 – 2033Combined sources
Helixi204 – 21613Combined sources
Beta strandi222 – 2298Combined sources
Helixi236 – 24813Combined sources
Beta strandi253 – 2597Combined sources
Beta strandi262 – 2643Combined sources
Helixi265 – 27915Combined sources
Beta strandi283 – 2886Combined sources
Helixi289 – 2913Combined sources
Helixi294 – 30310Combined sources
Beta strandi305 – 3106Combined sources
Helixi320 – 3223Combined sources
Helixi323 – 33210Combined sources
Beta strandi338 – 34811Combined sources
Helixi351 – 36111Combined sources
Beta strandi365 – 3673Combined sources
Beta strandi373 – 3775Combined sources
Helixi380 – 39718Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-399.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9FDN7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini255 – 394140Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 221190Zinc metallo-hydrolaseAdd
BLAST

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.
OrthoDBiEOG6BGP1J.

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
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. Positions 2-399.
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.
OrthoDBiEOG6BGP1J.

Enzyme and pathway databases

BioCyciMTHE264732:GH0A-1341-MONOMER.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Five-gene cluster in Clostridium thermoaceticum consisting of two divergent operons encoding rubredoxin oxidoreductase-rubredoxin and rubrerythrin-type A flavoprotein- high-molecular-weight rubredoxin."
    Das A., Coulter E.D., Kurtz D.M. Jr., Ljungdahl L.G.
    J. Bacteriol. 183:1560-1567(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39073.
  3. "A flavodiiron protein and high molecular weight rubredoxin from Moorella thermoacetica with nitric oxide reductase activity."
    Silaghi-Dumitrescu R., Coulter E.D., Das A., Ljungdahl L.G., Jameson G.N.L., Huynh B.H., Kurtz D.M. Jr.
    Biochemistry 42:2806-2815(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF FUNCTION, CHARACTERIZATION, COFACTOR.

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: January 20, 2016
This is version 102 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.