Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P24232 (HMP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Flavohemoprotein
Alternative name(s):
Flavohemoglobin
HMP
Hemoglobin-like protein
Nitric oxide dioxygenase
Short name=NO oxygenase
Short name=NOD
EC=1.14.12.17
Gene names
Name:hmp
Synonyms:fsrB, hmpA
Ordered Locus Names:b2552, JW2536
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.10 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25 Ref.30 Ref.33 Ref.34

In the presence of oxygen and NADH, HMP 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 HMP might act as an amplifier of superoxide stress. Under anaerobic conditions, HMP also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity. Ref.6 Ref.10 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25 Ref.30 Ref.33 Ref.34

Various electron acceptors are also reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if these reactions are of any biological significance in vivo. Ref.6 Ref.10 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25 Ref.30 Ref.33 Ref.34

Catalytic activity

2 nitric oxide + 2 O2 + NAD(P)H = 2 nitrate + NAD(P)+ + H+. Ref.30

Cofactor

Binds 1 FAD per subunit.

Binds 1 heme B group per subunit.

Subunit structure

Monomer.

Subcellular location

Cytoplasm. Note: Has also been found to localize into the periplasm, but spectral analysis revealed that biochemically active HMP is exclusively found in the cytoplasmic fraction. Ref.11

Induction

By nitric oxyde NO (under aerobic conditions), nitrite, nitrate (under anaerobic conditions), nitroso compounds, and paraquat. Ref.13 Ref.15 Ref.19

Domain

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. Ref.34

Miscellaneous

No protein-heme interactions have been detected at the distal side of the heme molecule.

HMP is able to bind specifically unsaturated and/or cyclopropanated fatty acids with high affinity.

Sequence similarities

Belongs to the globin family. Two-domain flavohemoproteins subfamily.

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Contains 1 FAD-binding FR-type domain.

Biophysicochemical properties

Kinetic parameters:

KM=0.28 µM for NO Ref.23

KM=90 µM for O2

KM=1.8 µM for NADH

KM=19.6 µM for NADPH

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396Flavohemoprotein HAMAP-Rule MF_01252
PRO_0000052431

Regions

Domain150 – 255106FAD-binding FR-type
Nucleotide binding204 – 2074FAD HAMAP-Rule MF_01252
Nucleotide binding268 – 2736NADP By similarity
Nucleotide binding389 – 3924FAD HAMAP-Rule MF_01252
Region1 – 138138Globin HAMAP-Rule MF_01252
Region147 – 396250Reductase HAMAP-Rule MF_01252
Region259 – 396138NAD or NADP-binding HAMAP-Rule MF_01252

Sites

Active site951Charge relay system Ref.28
Active site1351Charge relay system Ref.28
Metal binding851Iron (heme proximal ligand)
Binding site1881FAD
Site291Involved in heme-bound ligand stabilization and O-O bond activation
Site841Influences the redox potential of the prosthetic heme and FAD groups
Site3881Influences the redox potential of the prosthetic heme and FAD groups

Experimental info

Mutagenesis291Y → E or H: 15 to 35-fold reduction in NO dioxygenase activity. Ref.23
Mutagenesis291Y → F: 30-fold reduction in NO dioxygenase activity, and 80-fold increase in the O(2) dissociation rate constant. Ref.23

Secondary structure

......................................................... 396
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24232 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 49961BDE1444BD6B

FASTA39643,868
        10         20         30         40         50         60 
MLDAQTIATV KATIPLLVET GPKLTAHFYD RMFTHNPELK EIFNMSNQRN GDQREALFNA 

        70         80         90        100        110        120 
IAAYASNIEN LPALLPAVEK IAQKHTSFQI KPEQYNIVGE HLLATLDEMF SPGQEVLDAW 

       130        140        150        160        170        180 
GKAYGVLANV FINREAEIYN ENASKAGGWE GTRDFRIVAK TPRSALITSF ELEPVDGGAV 

       190        200        210        220        230        240 
AEYRPGQYLG VWLKPEGFPH QEIRQYSLTR KPDGKGYRIA VKREEGGQVS NWLHNHANVG 

       250        260        270        280        290        300 
DVVKLVAPAG DFFMAVADDT PVTLISAGVG QTPMLAMLDT LAKAGHTAQV NWFHAAENGD 

       310        320        330        340        350        360 
VHAFADEVKE LGQSLPRFTA HTWYRQPSEA DRAKGQFDSE GLMDLSKLEG AFSDPTMQFY 

       370        380        390 
LCGPVGFMQF TAKQLVDLGV KQENIHYECF GPHKVL 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12."
Vasudevan S.G., Armarego W.L.F., Shaw D.C., Lilley P.E., Dixon N.E., Poole R.K.
Mol. Gen. Genet. 226:49-58(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20.
Strain: K12.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Characterization of the Escherichia coli gene for serine hydroxymethyltransferase."
Plamann M.D., Stauffer G.V.
Gene 22:9-18(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
[6]"The haemoglobin-like protein (HMP) of Escherichia coli has ferrisiderophore reductase activity and its C-terminal domain shares homology with ferredoxin NADP+ reductases."
Andrews S.C., Shipley D., Keen J.N., Findlay J.B.C., Harrison P.M., Guest J.R.
FEBS Lett. 302:247-252(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION AS A FERRISIDEROPHORE REDUCTASE.
Strain: K12.
[7]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[8]"Nitric oxide dioxygenase: an enzymic function for flavohemoglobin."
Gardner P.R., Gardner A.M., Martin L.A., Salzman A.L.
Proc. Natl. Acad. Sci. U.S.A. 95:10378-10383(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-20, CHARACTERIZATION.
[9]"The oxygenated flavohaemoglobin from Escherichia coli: evidence from photodissociation and rapid-scan studies for two kinetic and spectral forms."
Orii Y., Ioannidis N., Poole R.K.
Biochem. Biophys. Res. Commun. 187:94-100(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: RAPID-SCAN AND FLASH PHOTOLYSIS SPECTROSCOPY.
[10]"Ferric reductases in Escherichia coli: the contribution of the haemoglobin-like protein."
Eschenbrenner M., Coves J., Fontecave M.
Biochem. Biophys. Res. Commun. 198:127-131(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A FERRIC CITRATE REDUCTASE.
[11]"Distribution of the flavohaemoglobin, HMP, between periplasm and cytoplasm in Escherichia coli."
Vasudevan S.G., Tang P., Dixon N.E., Poole R.K.
FEMS Microbiol. Lett. 125:219-224(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"The flavohaemoglobin (HMP) of Escherichia coli generates superoxide in vitro and causes oxidative stress in vivo."
Membrillo-Hernandez J., Ioannidis N., Poole R.K.
FEBS Lett. 382:141-144(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A NADH OXIDASE, ROLE IN OXIDATIVE STRESS.
[13]"Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12."
Poole R.K., Anjum M.F., Membrillo-Hernandez J., Kim S.O., Hughes M.N., Stewart V.
J. Bacteriol. 178:5487-5492(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTIONAL REGULATION.
Strain: K12.
[14]"Reactions of the Escherichia coli flavohaemoglobin (Hmp) with NADH and near-micromolar oxygen: oxygen affinity of NADH oxidase activity."
Poole R.K., Ioannidis N., Orii Y.
Microbiology 142:1141-1148(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A AEROBIC NADH OXIDASE AND ANAEROBIC FAD REDUCTASE.
[15]"Paraquat regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12 is SoxRS independent but modulated by sigma S."
Membrillo-Hernandez J., Kim S.O., Cook G.M., Poole R.K.
J. Bacteriol. 179:3164-3170(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTIONAL REGULATION.
Strain: K12.
[16]"Escherichia coli flavohaemoglobin (Hmp) reduces cytochrome c and Fe(III)-hydroxamate K by electron transfer from NADH via FAD: sensitivity of oxidoreductase activity to haem-bound dioxygen."
Poole R.K., Rogers N.J., D'mello R.A.M., Hughes M.N., Orii Y.
Microbiology 143:1557-1565(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A CYTOCHROME C REDUCTASE AND FERRISIDEROPHORE REDUCTASE.
[17]"Response of the NAD(P)H-oxidising flavohaemoglobin (Hmp) to prolonged oxidative stress and implications for its physiological role in Escherichia coli."
Anjum M.F., Ioannidis N., Poole R.K.
FEMS Microbiol. Lett. 166:219-223(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A NADH AND NADPH OXIDASE.
[18]"Constitutive and adaptive detoxification of nitric oxide in Escherichia coli. Role of nitric-oxide dioxygenase in the protection of aconitase."
Gardner P.R., Costantino G., Salzman A.L.
J. Biol. Chem. 273:26528-26533(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN NITRIC OXIDE DETOXIFICATION.
[19]"A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region."
Membrillo-Hernandez J., Coopamah M.D., Channa A., Hughes M.N., Poole R.K.
Mol. Microbiol. 29:1101-1112(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TRANSCRIPTIONAL REGULATION BY NITRIC OXIDE DONORS.
Strain: K12.
[20]"Nitrosative stress: metabolic pathway involving the flavohemoglobin."
Hausladen A., Gow A., Stamler J.S.
Proc. Natl. Acad. Sci. U.S.A. 95:14100-14105(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A NITRIC OXIDE DIOXYGENASE.
[21]"Anoxic function for the Escherichia coli flavohaemoglobin (Hmp): reversible binding of nitric oxide and reduction to nitrous oxide."
Kim S.O., Orii Y., Lloyd D., Hughes M.N., Poole R.K.
FEBS Lett. 445:389-394(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN ANAEROBIC NITRIC OXIDE REDUCTASE.
[22]"The flavohemoglobin of Escherichia coli confers resistance to a nitrosating agent, a 'nitric oxide releaser', and paraquat and is essential for transcriptional responses to oxidative stress."
Membrillo-Hernandez J., Coopamah M.D., Anjum M.F., Stevanin T.M., Kelly A., Hughes M.N., Poole R.K.
J. Biol. Chem. 274:748-754(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN RESISTANCE TO NITRIC OXIDE AND PARAQUAT.
[23]"Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis."
Gardner A.M., Martin L.A., Gardner P.R., Dou Y., Olson J.S.
J. Biol. Chem. 275:12581-12589(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-29.
[24]"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: CHARACTERIZATION.
[25]"Flavohemoglobin Hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo' or bd, from nitric oxide."
Stevanin T.M., Ioannidis N., Mills C.E., Kim S.O., Hughes M.N., Poole R.K.
J. Biol. Chem. 275:35868-35875(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN NITRIC OXIDE DETOXIFICATION.
[26]"Escherichia coli flavohaemoglobin (Hmp) with equistoichiometric FAD and haem contents has a low affinity for dioxygen in the absence or presence of nitric oxide."
Mills C.E., Sedelnikova S., Soeballe B., Hughes M.N., Poole R.K.
Biochem. J. 353:207-213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[27]"The distal heme pocket of Escherichia coli flavohemoglobin probed by infrared spectroscopy."
Bonamore A., Chiancone E., Boffi A.
Biochim. Biophys. Acta 1549:174-178(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INFRARED SPECTROSCOPY.
[28]"Flavohemoglobin, a globin with a peroxidase-like catalytic site."
Mukai M., Mills C.E., Poole R.K., Yeh S.-R.
J. Biol. Chem. 276:7272-7277(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE, RESONANCE RAMAN SPECTROSCOPY.
[29]"Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl equivalent with molecular oxygen."
Hausladen A., Gow A., Stamler J.S.
Proc. Natl. Acad. Sci. U.S.A. 98:10108-10112(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DENITROSYLASE ACTIVITY.
[30]"Flavohemoglobin detoxifies nitric oxide in aerobic, but not anaerobic, Escherichia coli. Evidence for a novel inducible anaerobic nitric oxide-scavenging activity."
Gardner A.M., Gardner P.R.
J. Biol. Chem. 277:8166-8171(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, ROLE IN AEROBIC NITRIC OXIDE DETOXIFICATION.
[31]"Interaction with membrane lipids and heme ligand binding properties of Escherichia coli flavohemoglobin."
Bonamore A., Farina A., Gattoni M., Schinina M.E., Bellelli A., Boffi A.
Biochemistry 42:5792-5801(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LIPIDS.
[32]"Escherichia coli flavohemoglobin is an efficient alkylhydroperoxide reductase."
Bonamore A., Gentili P., Ilari A., Schinina M.E., Boffi A.
J. Biol. Chem. 278:22272-22277(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ALKYLHYDROPEROXIDE REDUCTASE ACTIVITY.
[33]"Nitric oxide formation by Escherichia coli. Dependence on nitrite reductase, the NO-sensing regulator Fnr, and flavohemoglobin Hmp."
Corker H., Poole R.K.
J. Biol. Chem. 278:31584-31592(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN NITRIC OXIDE FORMATION.
[34]"Flavohemoglobin Hmp, but not its individual domains, confers protection from respiratory inhibition by nitric oxide in Escherichia coli."
Hernandez-Urzua E., Mills C.E., White G.P., Contreras-Zentella M.L., Escamilla E., Vasudevan S.G., Membrillo-Hernandez J., Poole R.K.
J. Biol. Chem. 278:34975-34982(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF SEPARATE FUNCTIONAL DOMAINS.
[35]"The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket."
Ilari A., Bonamore A., Farina A., Johnson K.A., Boffi A.
J. Biol. Chem. 277:23725-23732(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS).
[36]"New functions for the ancient globin family: bacterial responses to nitric oxide and nitrosative stress."
Poole R.K., Hughes M.N.
Mol. Microbiol. 36:775-783(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[37]"Bacterial hemoglobins and flavohemoglobins: versatile proteins and their impact on microbiology and biotechnology."
Frey A.D., Kallio P.T.
FEMS Microbiol. Rev. 27:525-545(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58872 Genomic DNA. Translation: CAA41682.1.
U00096 Genomic DNA. Translation: AAC75605.1.
AP009048 Genomic DNA. Translation: BAA16460.1.
J01620 Genomic DNA. Translation: AAA23911.1.
PIRS15992.
RefSeqNP_417047.1. NC_000913.3.
YP_490780.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GVHX-ray2.19A1-396[»]
ProteinModelPortalP24232.
SMRP24232. Positions 1-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP24232. 4 interactions.
STRING511145.b2552.

Proteomic databases

PaxDbP24232.
PRIDEP24232.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75605; AAC75605; b2552.
BAA16460; BAA16460; BAA16460.
GeneID12930206.
947018.
KEGGecj:Y75_p2505.
eco:b2552.
PATRIC32120503. VBIEscCol129921_2654.

Organism-specific databases

EchoBASEEB0451.
EcoGeneEG10456. hmp.

Phylogenomic databases

eggNOGCOG1018.
HOGENOMHOG000238921.
KOK05916.
OMADQYQIVG.
OrthoDBEOG64V2BB.
PhylomeDBP24232.

Enzyme and pathway databases

BioCycEcoCyc:EG10456-MONOMER.
ECOL316407:JW2536-MONOMER.
MetaCyc:EG10456-MONOMER.
SABIO-RKP24232.

Gene expression databases

GenevestigatorP24232.

Family and domain databases

Gene3D1.10.490.10. 1 hit.
HAMAPMF_01252. Hmp.
InterProIPR017927. 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]
PfamPF00970. FAD_binding_6. 1 hit.
PF00042. Globin. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00410. PHEHYDRXLASE.
SUPFAMSSF46458. SSF46458. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP24232.
PROP24232.

Entry information

Entry nameHMP_ECOLI
AccessionPrimary (citable) accession number: P24232
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 11, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene