Flavohemoprotein - Escherichia coli (strain K12)

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P24232 (HMP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 137. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Evidence 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 NO + 2 O₂ + NAD(P)H = 2 NO₃^- + NAD(P)⁺. 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. HAMAP-Rule MF_01252 HMP is able to bind specifically unsaturated and/or cyclopropanated fatty acids with high affinity. HAMAP-Rule MF_01252
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: K_M=0.28 µM for NO Ref.23 K_M=90 µM for O₂ K_M=1.8 µM for NADH K_M=19.6 µM for NADPH

Ontologies

Keywords
Biological process	Detoxification Oxygen transport Transport
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein Heme Iron Metal-binding NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	response to nitrosative stress Inferred from mutant phenotype Ref.22. Source: EcoCyc response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	FAD binding Inferred from direct assay PubMed 1334413. Source: EcoCyc fatty acid binding Inferred from direct assay Ref.31. Source: EcoCyc heme binding Inferred from direct assay PubMed 1334413 Ref.1. Source: EcoCyc hydroperoxide reductase activity Inferred from direct assay Ref.32. Source: EcoCyc iron ion binding Inferred from electronic annotation. Source: InterPro nitric oxide dioxygenase activity Inferred from direct assay Ref.23. Source: EcoCyc oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 396

396

Flavohemoprotein HAMAP-Rule MF_01252

PRO_0000052431

Regions

Domain

150 – 255

106

FAD-binding FR-type

Nucleotide binding

204 – 207

FAD HAMAP-Rule MF_01252

Nucleotide binding

268 – 273

NADP By similarity

Nucleotide binding

389 – 392

FAD HAMAP-Rule MF_01252

Region

1 – 138

138

Globin HAMAP-Rule MF_01252

Region

147 – 396

250

Reductase HAMAP-Rule MF_01252

Region

259 – 396

138

NAD or NADP-binding HAMAP-Rule MF_01252

Sites

Active site

Charge relay system Ref.28

Active site

135

Charge relay system Ref.28

Metal binding

Iron (heme proximal ligand)

Binding site

188

FAD

Site

Involved in heme-bound ligand stabilization and O-O bond activation

Site

Influences the redox potential of the prosthetic heme and FAD groups

Site

388

Influences the redox potential of the prosthetic heme and FAD groups

Experimental info

Mutagenesis

Y → E or H: 15 to 35-fold reduction in NO dioxygenase activity. Ref.23

Mutagenesis

Y → 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

Length

Mass (Da)

Tools

P24232 [UniParc].

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

FASTA

396

43,868

        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' referencesShow '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. 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 277:1453-1474(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.

PIR

S15992.

RefSeq

NP_417047.1. NC_000913.2.
YP_490780.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GVH	X-ray	2.19	A	1-396	[»]

ProteinModelPortal

P24232.

SMR

P24232. Positions 1-396.

ModBase

Search...

Protein-protein interaction databases

IntAct

P24232. 4 interactions.

STRING

511145.b2552.

Proteomic databases

PaxDb

P24232.

PRIDE

P24232.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75605; AAC75605; b2552.
BAA16460; BAA16460; BAA16460.

GeneID

12930206.
947018.

KEGG

ecj:Y75_p2505.
eco:b2552.

PATRIC

32120503. VBIEscCol129921_2654.

Organism-specific databases

EchoBASE

EB0451.

EcoGene

EG10456. hmp.

Phylogenomic databases

eggNOG

COG1018.

HOGENOM

HOG000238921.

K05916.

OMA

VAAYAKN.

ProtClustDB

PRK13289.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10456-MONOMER.
ECOL316407:JW2536-MONOMER.
MetaCyc:EG10456-MONOMER.

SABIO-RK

P24232.

Gene expression databases

Genevestigator

P24232.

Family and domain databases

Gene3D

1.10.490.10. 1 hit.

HAMAP

MF_01252. Hmp.

InterPro

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]

Pfam

PF00970. FAD_binding_6. 1 hit.
PF00042. Globin. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]

PRINTS

PR00410. PHEHYDRXLASE.

SUPFAM

SSF46458. Globin_like. 1 hit.
SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.

PROSITE

PS51384. FAD_FR. 1 hit.
PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P24232.

Entry information

Entry name

HMP_ECOLI

Accession

Primary (citable) accession number: P24232

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	May 1, 2013
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents