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P39662

- HMP_CUPNH

UniProt

P39662 - HMP_CUPNH

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Protein

Flavohemoprotein

Gene

hmp

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O2 and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.
In the presence of oxygen and NADH, FHP has NADH oxidase activity, which leads to the generation of superoxide and H2O2, both in vitro and in vivo, and it has been suggested that FHP might act as an amplifier of superoxide stress. Under anaerobic conditions, FHP also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity.

Catalytic activityi

2 nitric oxide + 2 O2 + NAD(P)H = 2 nitrate + NAD(P)+ + H+.1 Publication

Cofactori

Protein has several cofactor binding sites:

Kineticsi

  1. KM=0.10 µM for NO
  2. KM=80 µM for O2
  3. KM=70 µM for NADH

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei29 – 291Involved in heme-bound ligand stabilization and O-O bond activation
Sitei84 – 841Influences the redox potential of the prosthetic heme and FAD groups
Metal bindingi85 – 851Iron (heme proximal ligand)
Active sitei95 – 951Charge relay system
Active sitei137 – 1371Charge relay system
Binding sitei190 – 1901FAD
Sitei394 – 3941Influences the redox potential of the prosthetic heme and FAD groups

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi206 – 2094FAD
Nucleotide bindingi275 – 2806NADPBy similarity
Nucleotide bindingi395 – 3984FAD

GO - Molecular functioni

  1. FAD binding Source: InterPro
  2. heme binding Source: InterPro
  3. iron ion binding Source: InterPro
  4. nitric oxide dioxygenase activity Source: CACAO
  5. oxygen binding Source: InterPro
  6. oxygen transporter activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. response to nitrosative stress Source: InterPro
  2. response to toxic substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Detoxification, Oxygen transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, Heme, Iron, Metal-binding, NAD, NADP

Enzyme and pathway databases

BioCyciCNEC381666:GJUJ-6476-MONOMER.
SABIO-RKP39662.

Names & Taxonomyi

Protein namesi
Recommended name:
Flavohemoprotein
Alternative name(s):
FHP
Flavohemoglobin
Hemoglobin-like protein
Nitric oxide dioxygenase (EC:1.14.12.17)
Short name:
NO oxygenase
Short name:
NOD
Gene namesi
Name:hmp
Synonyms:fhp
Ordered Locus Names:PHG200
Encoded oniPlasmid megaplasmid pHG10 Publication
OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Taxonomic identifieri381666 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000008210: Plasmid megaplasmid pHG1

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601A → Y: Does not affect phospholipid-binding. 1 Publication
Mutagenesisi98 – 981V → F: Blocks phospholipid-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403FlavohemoproteinPRO_0000052441Add
BLAST

Expressioni

Inductioni

Under oxygen-limited conditions.1 Publication

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi381666.PHG200.

Structurei

Secondary structure

1
403
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1916Combined sources
Helixi21 – 3515Combined sources
Helixi37 – 415Combined sources
Helixi47 – 493Combined sources
Helixi50 – 6718Combined sources
Helixi71 – 8818Combined sources
Helixi92 – 943Combined sources
Helixi95 – 11016Combined sources
Helixi111 – 1133Combined sources
Helixi116 – 14530Combined sources
Beta strandi155 – 16410Combined sources
Beta strandi166 – 17611Combined sources
Beta strandi190 – 1967Combined sources
Turni198 – 2003Combined sources
Beta strandi201 – 2099Combined sources
Beta strandi219 – 2246Combined sources
Beta strandi229 – 2313Combined sources
Helixi235 – 2439Combined sources
Beta strandi249 – 2524Combined sources
Beta strandi269 – 2757Combined sources
Helixi278 – 28811Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi296 – 3038Combined sources
Beta strandi305 – 3073Combined sources
Helixi309 – 32012Combined sources
Beta strandi324 – 3329Combined sources
Turni339 – 3413Combined sources
Beta strandi344 – 3485Combined sources
Helixi351 – 3533Combined sources
Helixi355 – 3584Combined sources
Beta strandi364 – 3707Combined sources
Helixi371 – 38313Combined sources
Helixi388 – 3903Combined sources
Beta strandi391 – 3933Combined sources
Beta strandi396 – 3983Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQXX-ray1.75A/B1-403[»]
3OZUX-ray2.00A1-403[»]
3OZVX-ray2.40A/B1-403[»]
3OZWX-ray2.30A/B1-403[»]
ProteinModelPortaliP39662.
SMRiP39662. Positions 1-403.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39662.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini152 – 262111FAD-binding FR-typeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 140140GlobinAdd
BLAST
Regioni149 – 403255ReductaseAdd
BLAST
Regioni266 – 403138NAD or NADP-bindingAdd
BLAST

Domaini

Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.

Sequence similaritiesi

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Curated
Contains 1 FAD-binding FR-type domain.Curated

Phylogenomic databases

eggNOGiCOG1018.
HOGENOMiHOG000238921.
KOiK05916.
OMAiFNMAHQE.
OrthoDBiEOG64V2BB.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
HAMAPiMF_01252. Hmp.
InterProiIPR017927. Fd_Rdtase_FAD-bd.
IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR023950. Hmp.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00042. Globin. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00410. PHEHYDRXLASE.
SUPFAMiSSF46458. SSF46458. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS01033. GLOBIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39662-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLTQKTKDIV KATAPVLAEH GYDIIKCFYQ RMFEAHPELK NVFNMAHQEQ
60 70 80 90 100
GQQQQALARA VYAYAENIED PNSLMAVLKN IANKHASLGV KPEQYPIVGE
110 120 130 140 150
HLLAAIKEVL GNAATDDIIS AWAQAYGNLA DVLMGMESEL YERSAEQPGG
160 170 180 190 200
WKGWRTFVIR EKRPESDVIT SFILEPADGG PVVNFEPGQY TSVAIDVPAL
210 220 230 240 250
GLQQIRQYSL SDMPNGRSYR ISVKREGGGP QPPGYVSNLL HDHVNVGDQV
260 270 280 290 300
KLAAPYGSFH IDVDAKTPIV LISGGVGLTP MVSMLKVALQ APPRQVVFVH
310 320 330 340 350
GARNSAVHAM RDRLREAAKT YENLDLFVFY DQPLPEDVQG RDYDYPGLVD
360 370 380 390 400
VKQIEKSILL PDADYYICGP IPFMRMQHDA LKNLGIHEAR IHYEVFGPDL

FAE
Length:403
Mass (Da):44,782
Last modified:January 23, 2007 - v2
Checksum:i2E3ED365087F5EA0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti218 – 2181S → T in CAA52381. (PubMed:8125952)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74334 Genomic DNA. Translation: CAA52381.1.
AY305378 Genomic DNA. Translation: AAP85952.1.
PIRiA53396.
RefSeqiNP_942838.1. NC_005241.1.
WP_011154115.1. NC_005241.1.

Genome annotation databases

EnsemblBacteriaiAAP85952; AAP85952; PHG200.
GeneIDi2656642.
KEGGireh:PHG200.
PATRICi35228958. VBIRalEut6770_0150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74334 Genomic DNA. Translation: CAA52381.1 .
AY305378 Genomic DNA. Translation: AAP85952.1 .
PIRi A53396.
RefSeqi NP_942838.1. NC_005241.1.
WP_011154115.1. NC_005241.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CQX X-ray 1.75 A/B 1-403 [» ]
3OZU X-ray 2.00 A 1-403 [» ]
3OZV X-ray 2.40 A/B 1-403 [» ]
3OZW X-ray 2.30 A/B 1-403 [» ]
ProteinModelPortali P39662.
SMRi P39662. Positions 1-403.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 381666.PHG200.

Chemistry

DrugBanki DB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAP85952 ; AAP85952 ; PHG200 .
GeneIDi 2656642.
KEGGi reh:PHG200.
PATRICi 35228958. VBIRalEut6770_0150.

Phylogenomic databases

eggNOGi COG1018.
HOGENOMi HOG000238921.
KOi K05916.
OMAi FNMAHQE.
OrthoDBi EOG64V2BB.

Enzyme and pathway databases

BioCyci CNEC381666:GJUJ-6476-MONOMER.
SABIO-RK P39662.

Miscellaneous databases

EvolutionaryTracei P39662.

Family and domain databases

Gene3Di 1.10.490.10. 1 hit.
HAMAPi MF_01252. Hmp.
InterProi IPR017927. Fd_Rdtase_FAD-bd.
IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR023950. Hmp.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF00970. FAD_binding_6. 1 hit.
PF00042. Globin. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view ]
PRINTSi PR00410. PHEHYDRXLASE.
SUPFAMi SSF46458. SSF46458. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS51384. FAD_FR. 1 hit.
PS01033. GLOBIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary sequence and evidence for a physiological function of the flavohemoprotein of Alcaligenes eutrophus."
    Cramm R., Siddiqui R.A., Friedrich B.
    J. Biol. Chem. 269:7349-7354(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis."
    Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.
    J. Mol. Biol. 332:369-383(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.
  3. "Yeast flavohemoglobin is an ancient protein related to globins and a reductase family."
    Zhu H., Riggs A.F.
    Proc. Natl. Acad. Sci. U.S.A. 89:5015-5019(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  4. "An oxygen-binding flavohemoprotein from Alcaligenes eutrophus."
    Probst I., Wolf G., Schlegel H.G.
    Biochim. Biophys. Acta 576:471-478(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, INDUCTION, SPECTRAL PROPERTIES.
  5. "Nitric-oxide dioxygenase activity and function of flavohemoglobins. Sensitivity to nitric oxide and carbon monoxide inhibition."
    Gardner P.R., Gardner A.M., Martin L.A., Dou Y., Li T., Olson J.S., Zhu H., Riggs A.F.
    J. Biol. Chem. 275:31581-31587(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY.
  6. "Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75-A resolution."
    Ermler U., Siddiqui R.A., Cramm R., Friedrich B.
    EMBO J. 14:6067-6077(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
  7. "Phospholipid bound to the flavohemoprotein from Alcaligenes eutrophus."
    Ollesch G., Kaunzinger A., Juchelka D., Schubert-Zsilavecz M., Ermler U.
    Eur. J. Biochem. 262:396-405(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF NATIVE PROTEIN AND MUTANT V98F, PHOSPHOLIPID BINDING, MUTAGENESIS OF ALA-60 AND VAL-98.

Entry informationi

Entry nameiHMP_CUPNH
AccessioniPrimary (citable) accession number: P39662
Secondary accession number(s): Q7WXD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

No protein-heme interactions have been detected at the distal side of the heme molecule.
FHP is able to bind phospholipids with high affinity.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Plasmid, Reference proteome

Documents

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

External Data

Dasty 3