ID I2GZK4_TETBL Unreviewed; 398 AA.
AC I2GZK4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229};
DE EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229};
GN Name=TBLA0B07380 {ECO:0000313|EMBL:CCH59556.1};
GN ORFNames=TBLA_0B07380 {ECO:0000313|EMBL:CCH59556.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH59556.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH59556.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00238}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family.
CC {ECO:0000256|ARBA:ARBA00006401}.
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DR EMBL; HE806317; CCH59556.1; -; Genomic_DNA.
DR RefSeq; XP_004179075.1; XM_004179027.1.
DR AlphaFoldDB; I2GZK4; -.
DR GeneID; 14494345; -.
DR KEGG; tbl:TBLA_0B07380; -.
DR eggNOG; KOG3378; Eukaryota.
DR HOGENOM; CLU_003827_12_0_1; -.
DR InParanoid; I2GZK4; -.
DR OMA; KLERMCN; -.
DR OrthoDB; 2096069at2759; -.
DR Proteomes; UP000002866; Chromosome 2.
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:0062197; P:cellular response to chemical stress; IEA:UniProt.
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; 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; 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; PF00970; FAD_binding_6; 1.
DR Pfam; PF00042; Globin; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
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 Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002866}.
FT DOMAIN 1..138
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
FT DOMAIN 147..263
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 398 AA; 44882 MW; 2FD4D08CD93A61EB CRC64;
MLPEQVRTII KATVPVLEQH GTTITKTFYK NMLNDHNELR NVFNRTNQMR GAQPNALATT
VLAAAKHIDD LSPLLTHVRQ IGHKHRALQI YPEQYDIVGE YLIKAIQQVL GPAATPQIID
AWTKAYGEIA NVFIDVEKQM YKEAMWPGWK KFLVSAMEPV GTNVIKFTVT PKNPTDIILK
NLPIEAGQYI TVKTHPIRQD NKYDALRHYS LCSSLHDENL KFSVKLEQTE NLPNGLVSEY
LDLDVKVGDE LELSAPAGDF TMNKDLIMQD KVPLVLLAAG VGATPLLAML ETQIRNYPSR
PIYWFQSSQD EASEVFKKEV DGLLKNASSV KKVVVHTNKQ PEIDAKFLKE NIPEGADVYL
CGPLGFMKGM VDHFKVLEFK KDDIHYEPFG PKMSTVKV
//
