Flavohemoprotein - Salmonella typhimurium

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Reviewed, UniProtKB/Swiss-Prot P26353 (HMP_SALTY)

Last modified January 19, 2010. Version 94. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Flavohemoprotein
Alternative name(s):
    Hemoglobin-like protein
    Flavohemoglobin
    Nitric oxide dioxygenase
      Short name=NO oxygenase
      Short name=NOD
    EC=1.14.12.17

Gene names

Name:	hmp
Synonyms:	frsB, hmpA
Ordered Locus Names:	STM2556

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

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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.1 Ref.5
Catalytic activity	2 NO + 2 O₂ + NAD(P)H = 2 NO₃^- + NAD(P)⁺. HAMAP MF_01252
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. HAMAP MF_01252 Binds 1 FAD per subunit By similarity. HAMAP MF_01252
Subunit structure	Monomer. HAMAP MF_01252
Induction	By nitric oxide. Ref.4
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. HAMAP 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.

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Ontologies

Keywords
Biological process	Detoxification Oxygen transport Transport
Ligand	FAD Flavoprotein Heme Iron Metal-binding NAD NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen transport Inferred from electronic annotation. Source: HAMAP response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro nitric oxide dioxygenase activity Inferred from electronic annotation. Source: HAMAP oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 396

396

Flavohemoprotein HAMAP MF_01252

PRO_0000052447

Regions

Domain

150 – 255

106

FAD-binding FR-type

Nucleotide binding

204 – 207

FAD By similarity

Nucleotide binding

268 – 273

NADP By similarity

Nucleotide binding

389 – 392

FAD By similarity

Region

1 – 138

138

Globin HAMAP MF_01252

Region

147 – 396

250

Reductase HAMAP MF_01252

Region

259 – 396

138

NAD or NADP-binding HAMAP MF_01252

Sites

Active site

Charge relay system By similarity

Active site

135

Charge relay system By similarity

Metal binding

Iron (heme proximal ligand) By similarity

Binding site

188

FAD By similarity

Site

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

Site

Influences the redox potential of the prosthetic heme and FAD groups By similarity

Site

388

Influences the redox potential of the prosthetic heme and FAD groups By similarity

Experimental info

Sequence conflict

202 – 203

EI → VF in AAC24484. Ref.1

Sequence conflict

242

G → V in AAC24484. Ref.1

Sequence conflict

330

S → A in AAC24484. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P26353-1 [UniParc].

Last modified January 23, 2002. Version 3.
Checksum: 90D0FBCB239C87C5
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FASTA

396

43,992

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

        70         80         90        100        110        120 
IAAYASNIEN LPALLPAVEK IAQKHTSFQI KPEQYNIVGT HLLATLDEMF NPGQEVLDAW 

       130        140        150        160        170        180 
GKAYGVLANV FIHREAEIYH ENASKDGGWE GTRPFRIVAK TPRSALITSF EFEPVDGGTV 

       190        200        210        220        230        240 
AEYRPGQYLG VWLKPEGFAH QEIRQYSLTR KPDGKGYRIA VKREDGGQVS NWLHHHASVG 

       250        260        270        280        290        300 
DGVHLAAPAG DFFMNVAADT PVSLISAGVG QTPMLAMLDT LAKEQHTAQV NWFHAAENGD 

       310        320        330        340        350        360 
VHAFADEVSE LGRTLPRFTA HTWYREPTES DRAQRLFDSE GLMDLSKLEA AISDPAMQFY 

       370        380        390 
LCGPVGFMQF AAKQLVSLGV NNENIHYECF GPHKVL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Role for the Salmonella flavohemoglobin in protection from nitric oxide." Crawford M.J., Goldberg D.E. J. Biol. Chem. 273:12543-12547(1998) [PubMed: 9575213] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ROLE IN RESISTANCE TO NITRIC OXIDE. Strain: ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"Nucleotide sequence of the Salmonella typhimurium glyA gene." Steiert J.G., Urbanowski M.L., Stauffer L.T., Plamann M.D., Stauffer G.V. DNA Seq. 1:107-113(1990) [PubMed: 2134182] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29. Strain: LT2.
[4]	"Regulation of the Salmonella typhimurium flavohemoglobin gene. A new pathway for bacterial gene expression in response to nitric oxide." Crawford M.J., Goldberg D.E. J. Biol. Chem. 273:34028-34032(1998) [PubMed: 9852058] [Abstract] Cited for: INDUCTION.
[5]	"Flavohemoglobin Hmp protects Salmonella enterica serovar typhimurium from nitric oxide-related killing by human macrophages." Stevanin T.M., Poole R.K., Demoncheaux E.A.G., Read R.C. Infect. Immun. 70:4399-4405(2002) [PubMed: 12117950] [Abstract] Cited for: ROLE IN NITRIC OXIDE DETOXIFICATION.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AF020388 Genomic DNA. Translation: AAC24484.1. AE006468 Genomic DNA. Translation: AAL21450.1. X15816 Genomic DNA. No translation available.
PIR	A48427.
RefSeq	NP_461491.1.
3D structure databases
SMR	P26353. Positions 1-396.
ModBase	Search...
Proteomic databases
PRIDE	P26353.
Genome annotation databases
GeneID	1254078.
GenomeReviews	Gene locus STM2556 in contig AE006468_GR.
KEGG	stm:STM2556.
NMPDR	fig\|99287.1.peg.2470.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG623097.
OMA	KQIGHKH.
Enzyme and pathway databases
BioCyc	STYP99287:STM2556-MONOMER.
BRENDA	1.14.12.17. 2.
Family and domain databases
HAMAP	MF_01252. Hmp. [Tree]
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR012292. Globin. IPR009050. Globin-like. IPR000971. Globin_subset. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD_bd. IPR001221. Phe_hydroxylase. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Gene3D	G3DSA:1.10.490.10. Globin_related. 1 hit.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00042. Globin. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00410. PHEHYDRXLASE.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

HMP_SALTY

Accession

Primary (citable) accession number: P26353

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2002
Last modified:	January 19, 2010
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents