FHBB_DICDI
ID FHBB_DICDI Reviewed; 423 AA.
AC Q54D73; Q9UAG6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Flavohemoprotein B;
DE EC=1.14.12.17;
DE AltName: Full=DdFHb;
DE AltName: Full=Flavohemoglobin B;
DE AltName: Full=Hemoglobin-like protein B;
DE AltName: Full=Nitric oxide dioxygenase B;
DE Short=NO oxygenase B;
DE Short=NOD B;
GN Name=fhbB; ORFNames=DDB_G0292380;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=AX3-1;
RX PubMed=10791894; DOI=10.1247/csf.25.47;
RA Iijima M., Shimizu H., Tanaka Y., Urushihara H.;
RT "Identification and characterization of two flavohemoglobin genes in
RT Dictyostelium discoideum.";
RL Cell Struct. Funct. 25:47-55(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
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 cell from various
CC noxious nitrogen compounds. Therefore, plays a central role in the
CC inducible response to nitrosative stress.
CC {ECO:0000269|PubMed:10791894}.
CC -!- FUNCTION: In the presence of oxygen and NADH, it has NADH oxidase
CC activity, which leads to the generation of superoxide and H(2)O(2).
CC Under anaerobic conditions, it also exhibits nitric oxide reductase and
CC FAD reductase activities. However, all these reactions are much lower
CC than NOD activity (By similarity). {ECO:0000250}.
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=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 heme b group per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in macrocysts.
CC {ECO:0000269|PubMed:10791894}.
CC -!- INDUCTION: By submerged conditions, in growing cells.
CC {ECO:0000269|PubMed:10791894}.
CC -!- DOMAIN: Consists of two distinct domains; a 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|PROSITE-ProRule:PRU00238}.
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; AB025584; BAA83811.1; -; mRNA.
DR EMBL; AAFI02000190; EAL61169.1; -; Genomic_DNA.
DR RefSeq; XP_629623.1; XM_629621.1.
DR AlphaFoldDB; Q54D73; -.
DR SMR; Q54D73; -.
DR STRING; 44689.DDB0191088; -.
DR PaxDb; Q54D73; -.
DR EnsemblProtists; EAL61169; EAL61169; DDB_G0292380.
DR GeneID; 8628686; -.
DR KEGG; ddi:DDB_G0292380; -.
DR dictyBase; DDB_G0292380; fhbB.
DR eggNOG; KOG3378; Eukaryota.
DR HOGENOM; CLU_003827_12_0_1; -.
DR InParanoid; Q54D73; -.
DR OMA; EICAAWG; -.
DR PhylomeDB; Q54D73; -.
DR PRO; PR:Q54D73; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
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-KW.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IMP:dictyBase.
DR GO; GO:0071500; P:cellular response to nitrosative stress; IGI:dictyBase.
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 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; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
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 1: Evidence at protein level;
KW Cytoplasm; Detoxification; FAD; Flavoprotein; Heme; Iron; Metal-binding;
KW NAD; NADP; Oxidoreductase; Oxygen transport; Reference proteome; Transport.
FT CHAIN 1..423
FT /note="Flavohemoprotein B"
FT /id="PRO_0000327850"
FT DOMAIN 150..268
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..140
FT /note="Globin"
FT REGION 149..423
FT /note="Reductase"
FT /evidence="ECO:0000250"
FT ACT_SITE 93
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 135
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 83
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|PROSITE-ProRule:PRU00238"
FT BINDING 188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 212..215
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 281..286
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 400..403
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 82
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000250"
FT SITE 399
FT /note="Influences the redox potential of the prosthetic
FT heme and FAD groups"
FT /evidence="ECO:0000250"
FT CONFLICT 366
FT /note="A -> D (in Ref. 1; BAA83811)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 48206 MW; 3768C17E89D6D70C CRC64;
MLSQKSIQII KSTVPLLEKY GVEITSLFYK NMFEAQPQFL NIFNHSNQRN QKQPVALANT
ILQSAIHIEK LNEINLMPIV HKHVALGITP EMYPIVGAHL LGAMKTVMQD EATPEIMAAW
TEAYRAVAQA FMDAEEDLYF ETEEQIGGWK DTREFVVDRI EEETPLIKSF YFKAYDGKEI
ATYIPGQYIT VKITLPGDGV DVPTDKMRTY VRHYSLSDKP NDEYYRISIK KELGKNTPNG
IVSNHFHNNI KVGDVVPMSV PAGDFVVNND SETPILLICG GVGINPLFSM LKETLVQQPD
RKINFIFSTH CESSQPFKEE LKQLEDDYKE TGNLKINLVY SENQGHINKE IIEKYSTQHV
DQAEIAETDV YICGPVPFMM QVNKDLLQLG FHKENVHYEL FGPLTPVLEE NQMLRGVKNI
IEN
