HMP_BACAN
ID HMP_BACAN Reviewed; 402 AA.
AC Q81T23; Q6I1A5; Q6KV53;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Flavohemoprotein {ECO:0000255|HAMAP-Rule:MF_01252};
DE AltName: Full=Flavohemoglobin {ECO:0000255|HAMAP-Rule:MF_01252};
DE AltName: Full=Hemoglobin-like protein {ECO:0000255|HAMAP-Rule:MF_01252};
DE AltName: Full=Nitric oxide dioxygenase {ECO:0000255|HAMAP-Rule:MF_01252};
DE Short=NO oxygenase {ECO:0000255|HAMAP-Rule:MF_01252};
DE Short=NOD {ECO:0000255|HAMAP-Rule:MF_01252};
DE EC=1.14.12.17 {ECO:0000255|HAMAP-Rule:MF_01252};
GN Name=hmp {ECO:0000255|HAMAP-Rule:MF_01252};
GN OrderedLocusNames=BA_1467, GBAA_1467, BAS1357;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC Rule:MF_01252}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01252};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01252};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01252};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01252};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01252};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01252};
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:0000255|HAMAP-Rule:MF_01252}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_01252}.
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DR EMBL; AE016879; AAP25408.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT30564.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53677.1; -; Genomic_DNA.
DR RefSeq; NP_843922.1; NC_003997.3.
DR RefSeq; WP_000947716.1; NZ_WXXJ01000014.1.
DR RefSeq; YP_027626.1; NC_005945.1.
DR AlphaFoldDB; Q81T23; -.
DR SMR; Q81T23; -.
DR STRING; 261594.GBAA_1467; -.
DR DNASU; 1084422; -.
DR EnsemblBacteria; AAP25408; AAP25408; BA_1467.
DR EnsemblBacteria; AAT30564; AAT30564; GBAA_1467.
DR GeneID; 45021446; -.
DR KEGG; ban:BA_1467; -.
DR KEGG; bar:GBAA_1467; -.
DR KEGG; bat:BAS1357; -.
DR PATRIC; fig|198094.11.peg.1440; -.
DR eggNOG; COG1017; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_12_0_9; -.
DR OMA; ADIHYEV; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051409; P:response to nitrosative stress; IEA:InterPro.
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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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 PRINTS; PR00371; FPNCR.
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 3: Inferred from homology;
KW Detoxification; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP;
KW Oxidoreductase; Oxygen transport; Reference proteome; Transport.
FT CHAIN 1..402
FT /note="Flavohemoprotein"
FT /id="PRO_0000052419"
FT DOMAIN 150..260
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT REGION 1..136
FT /note="Globin"
FT REGION 147..402
FT /note="Reductase"
FT ACT_SITE 95
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT ACT_SITE 135
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
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:0000255|HAMAP-Rule:MF_01252"
FT BINDING 188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT BINDING 204..207
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT BINDING 273..278
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT BINDING 394..397
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT SITE 29
FT /note="Involved in heme-bound ligand stabilization and O-O
FT bond activation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT SITE 84
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
FT SITE 393
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01252"
SQ SEQUENCE 402 AA; 45007 MW; 48FE39819B630DC1 CRC64;
MLSEKTIEIV KSTVPLLQEK GVEITTRFYE ILFSEHPELL NIFNHTNQKK GRQQQALANA
VYAAATYIDN LEAIIPVVKQ IGHKHRSLGI KAEHYPIVGT CLLRAIKEVA GAPDEVLNAW
GEAYGVIADA FISIEAEMYE EAAHKEGGWK DFRNFVVVKK VKESDVITSL YLKPEDGGKV
SSFIPGQYVT VQINIEGETY THNRQYSLSD APGKEYYRIS VKKEKGVDTP DGKVSNYLHD
HVKEGDMLPV SAPAGDFVLN MDSTLPVVLI SGGVGITPMM SMLNTLIEQD SKRNVCFVHA
AINSNTHAMK EHVEAVDNEY EQVKAYTCYS APTEKDLEMK NFDKEGFVER EWLQTIIPTT
EAEFYFCGPV PFMKHINAVL TDLGVKQEHI HYEFFGPAAS LQ
