HMP_SALTY
ID HMP_SALTY Reviewed; 396 AA.
AC P26353;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Flavohemoprotein;
DE AltName: Full=Flavohemoglobin;
DE AltName: Full=Hemoglobin-like protein;
DE AltName: Full=Nitric oxide dioxygenase;
DE Short=NO oxygenase;
DE Short=NOD;
DE EC=1.14.12.17;
GN Name=hmp; Synonyms=frsB, hmpA; OrderedLocusNames=STM2556;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ROLE IN RESISTANCE TO NITRIC OXIDE.
RC STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=9575213; DOI=10.1074/jbc.273.20.12543;
RA Crawford M.J., Goldberg D.E.;
RT "Role for the Salmonella flavohemoglobin in protection from nitric oxide.";
RL J. Biol. Chem. 273:12543-12547(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RC STRAIN=LT2;
RX PubMed=2134182; DOI=10.3109/10425179009016038;
RA Steiert J.G., Urbanowski M.L., Stauffer L.T., Plamann M.D., Stauffer G.V.;
RT "Nucleotide sequence of the Salmonella typhimurium glyA gene.";
RL DNA Seq. 1:107-113(1990).
RN [4]
RP INDUCTION.
RX PubMed=9852058; DOI=10.1074/jbc.273.51.34028;
RA Crawford M.J., Goldberg D.E.;
RT "Regulation of the Salmonella typhimurium flavohemoglobin gene. A new
RT pathway for bacterial gene expression in response to nitric oxide.";
RL J. Biol. Chem. 273:34028-34032(1998).
RN [5]
RP ROLE IN NITRIC OXIDE DETOXIFICATION.
RX PubMed=12117950; DOI=10.1128/iai.70.8.4399-4405.2002;
RA Stevanin T.M., Poole R.K., Demoncheaux E.A.G., Read R.C.;
RT "Flavohemoglobin Hmp protects Salmonella enterica serovar typhimurium from
RT nitric oxide-related killing by human macrophages.";
RL Infect. Immun. 70:4399-4405(2002).
CC -!- FUNCTION: Is involved in NO detoxification in an aerobic process,
CC termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and
CC NAD(P)H to convert NO to nitrate, which protects the bacterium from
CC various noxious nitrogen compounds. Therefore, plays a central role in
CC the inducible response to nitrosative stress.
CC {ECO:0000269|PubMed:12117950, ECO:0000269|PubMed:9575213}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 nitric oxide + 2 O2 = H(+) + NADP(+) + 2 nitrate;
CC Xref=Rhea:RHEA:19465, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.12.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADH + 2 nitric oxide + 2 O2 = H(+) + NAD(+) + 2 nitrate;
CC Xref=Rhea:RHEA:19469, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.14.12.17;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer.
CC -!- INDUCTION: By nitric oxide. {ECO:0000269|PubMed:9852058}.
CC -!- DOMAIN: Consists of two distinct domains; an N-terminal heme-containing
CC oxygen-binding domain and a C-terminal reductase domain with binding
CC sites for FAD and NAD(P)H.
CC -!- SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins
CC subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000305}.
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DR EMBL; AF020388; AAC24484.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21450.1; -; Genomic_DNA.
DR EMBL; X15816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A48427; A48427.
DR RefSeq; NP_461491.1; NC_003197.2.
DR RefSeq; WP_000883144.1; NC_003197.2.
DR AlphaFoldDB; P26353; -.
DR SMR; P26353; -.
DR STRING; 99287.STM2556; -.
DR PaxDb; P26353; -.
DR PRIDE; P26353; -.
DR EnsemblBacteria; AAL21450; AAL21450; STM2556.
DR GeneID; 1254078; -.
DR KEGG; stm:STM2556; -.
DR PATRIC; fig|99287.12.peg.2697; -.
DR HOGENOM; CLU_003827_12_0_6; -.
DR PhylomeDB; P26353; -.
DR BioCyc; SENT99287:STM2556-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008941; F:nitric oxide dioxygenase activity; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071500; P:cellular response to nitrosative stress; IBA:GO_Central.
DR GO; GO:0046210; P:nitric oxide catabolic process; IBA:GO_Central.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 1.10.490.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_01252; Hmp; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR023950; Hmp.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43396:SF3; PTHR43396:SF3; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00042; Globin; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 2: Evidence at transcript level;
KW Detoxification; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP;
KW Oxidoreductase; Oxygen transport; Reference proteome; Transport.
FT CHAIN 1..396
FT /note="Flavohemoprotein"
FT /id="PRO_0000052447"
FT DOMAIN 150..255
FT /note="FAD-binding FR-type"
FT REGION 1..138
FT /note="Globin"
FT REGION 147..396
FT /note="Reductase"
FT ACT_SITE 95
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 135
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 204..207
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 268..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 389..392
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT SITE 29
FT /note="Involved in heme-bound ligand stabilization and O-O
FT bond activation"
FT /evidence="ECO:0000250"
FT SITE 84
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000250"
FT SITE 388
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000250"
FT CONFLICT 202..203
FT /note="EI -> VF (in Ref. 1; AAC24484)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="G -> V (in Ref. 1; AAC24484)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="S -> A (in Ref. 1; AAC24484)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 43992 MW; 90D0FBCB239C87C5 CRC64;
MLDAQTIATV KATIPLLVET GPKLTAHFYD RMFTHNPELK EIFNMSNQRN GDQREALFNA
IAAYASNIEN LPALLPAVEK IAQKHTSFQI KPEQYNIVGT HLLATLDEMF NPGQEVLDAW
GKAYGVLANV FIHREAEIYH ENASKDGGWE GTRPFRIVAK TPRSALITSF EFEPVDGGTV
AEYRPGQYLG VWLKPEGFAH QEIRQYSLTR KPDGKGYRIA VKREDGGQVS NWLHHHASVG
DGVHLAAPAG DFFMNVAADT PVSLISAGVG QTPMLAMLDT LAKEQHTAQV NWFHAAENGD
VHAFADEVSE LGRTLPRFTA HTWYREPTES DRAQRLFDSE GLMDLSKLEA AISDPAMQFY
LCGPVGFMQF AAKQLVSLGV NNENIHYECF GPHKVL
