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Database: UniProt
Entry: K6VH56_9MICO
LinkDB: K6VH56_9MICO
Original site: K6VH56_9MICO 
ID   K6VH56_9MICO            Unreviewed;       404 AA.
AC   K6VH56;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE            EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN   Name=hmp {ECO:0000313|EMBL:GAB95538.1};
GN   ORFNames=KILIM_022_00220 {ECO:0000313|EMBL:GAB95538.1};
OS   Kineosphaera limosa NBRC 100340.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC   Kineosphaera.
OX   NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB95538.1, ECO:0000313|Proteomes:UP000008366};
RN   [1] {ECO:0000313|EMBL:GAB95538.1, ECO:0000313|Proteomes:UP000008366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB95538.1,
RC   ECO:0000313|Proteomes:UP000008366};
RA   Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y.,
RA   Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000126};
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         Evidence={ECO:0000256|ARBA:ARBA00001762};
CC   -!- SIMILARITY: Belongs to the globin family.
CC       {ECO:0000256|RuleBase:RU000356}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
CC       {ECO:0000256|ARBA:ARBA00006401}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAB95538.1}.
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DR   EMBL; BAHD01000022; GAB95538.1; -; Genomic_DNA.
DR   RefSeq; WP_006592070.1; NZ_BAHD01000022.1.
DR   AlphaFoldDB; K6VH56; -.
DR   STRING; 1184609.KILIM_022_00220; -.
DR   eggNOG; COG1017; Bacteria.
DR   eggNOG; COG1018; Bacteria.
DR   OrthoDB; 9801223at2; -.
DR   Proteomes; UP000008366; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0008941; F:nitric oxide dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   CDD; cd14782; FHb-globin_2; 1.
DR   CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR   Gene3D; 1.10.490.10; Globins; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
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   PANTHER; PTHR43396; FLAVOHEMOPROTEIN; 1.
DR   PANTHER; PTHR43396:SF3; FLAVOHEMOPROTEIN; 1.
DR   Pfam; PF00042; Globin; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF46458; Globin-like; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|RuleBase:RU000356}; Iron {ECO:0000256|RuleBase:RU000356};
KW   Metal-binding {ECO:0000256|RuleBase:RU000356};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxygen transport {ECO:0000256|RuleBase:RU000356};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008366};
KW   Transport {ECO:0000256|RuleBase:RU000356}.
FT   DOMAIN          6..129
FT                   /note="Globin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS01033"
FT   DOMAIN          153..261
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   404 AA;  44405 MW;  CF572BC66D80CB1D CRC64;
     MKLSPESEAI VKATAGVVAE HAEDITKVFY PDMFAAHPEL MRVFNKANQA IGEQPKALAA
     SVVAYAVNLI DPDAPDFGPV MRRIAHKHVS LGIRAQEYTI VGHHLLKAVK TVLGDAITPE
     VGAAWDEVYW LFGTELIAEE AKLYALAGTD PTHPWRKYRV VERFDEGEDV FSLVLSPVEG
     EAPPHEVGQY VAIAVDLPNG ERQPRQYTIS SSPRGDLRVT IKRVHGVDGA PEGQVSNWLY
     DNARPGTILD LSQPAGDLVL DDSTGPLVLV SAGIGITPIA AILDDLSRRQ PERTVRLFHA
     DTSHANHALY KHLRRQVEWM SDAKAQNWYE EGAEDAPTIH PARSGFMDLS DIAVPSDCTV
     FMCGPLEFMR SARRALLDKG VSSERIHYEV FGPDLWAQNP DNAA
//
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