ID A6ZUP2_YEAS7 Unreviewed; 399 AA. AC A6ZUP2; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=nitric oxide dioxygenase {ECO:0000256|ARBA:ARBA00012229}; DE EC=1.14.12.17 {ECO:0000256|ARBA:ARBA00012229}; GN Name=YHB1 {ECO:0000313|EMBL:EDN61819.1}; GN ORFNames=SCY_2125 {ECO:0000313|EMBL:EDN61819.1}; OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=307796 {ECO:0000313|EMBL:EDN61819.1, ECO:0000313|Proteomes:UP000007060}; RN [1] {ECO:0000313|EMBL:EDN61819.1, ECO:0000313|Proteomes:UP000007060} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YJM789 {ECO:0000313|EMBL:EDN61819.1, RC ECO:0000313|Proteomes:UP000007060}; RX PubMed=17652520; DOI=10.1073/pnas.0701291104; RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z., RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X., RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W., RA Steinmetz L.M.; RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae RT strain YJM789."; RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007). RN [2] {ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FAD AND HEME, AND RP DISULFIDE BONDS. RX PubMed=23095020; DOI=10.1111/febs.12043; RA El Hammi E., Warkentin E., Demmer U., Marzouki N.M., Ermler U., Baciou L.; RT "Active site analysis of yeast flavohemoglobin based on its structure with RT a small ligand or econazole."; RL FEBS J. 279:4565-4575(2012). 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}. 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:EDN61819.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAFW02000100; EDN61819.1; -; Genomic_DNA. DR PDB; 4G1B; X-ray; 3.00 A; A/B/C/D=1-399. DR PDB; 4G1V; X-ray; 2.10 A; A=1-399. DR PDBsum; 4G1B; -. DR PDBsum; 4G1V; -. DR AlphaFoldDB; A6ZUP2; -. DR SMR; A6ZUP2; -. DR HOGENOM; CLU_003827_12_0_1; -. DR Proteomes; UP000007060; Unassembled WGS sequence. 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-EC. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. 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 CDD; cd14777; Yhb1-globin-like; 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V}; KW FAD {ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0007829|PDB:4G1B}; KW Heme {ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V}; KW Iron {ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V}; KW Metal-binding {ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V}; KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857}; KW Nucleotide-binding {ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}. FT DOMAIN 9..138 FT /note="Globin family profile" FT /evidence="ECO:0000259|PROSITE:PS01033" FT DOMAIN 147..264 FT /note="FAD-binding FR-type" FT /evidence="ECO:0000259|PROSITE:PS51384" FT BINDING 44 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4G1B" FT BINDING 44 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4G1B" FT BINDING 47 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4G1V" FT BINDING 47 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4G1B" FT BINDING 80 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4G1V" FT BINDING 80 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4G1B" FT BINDING 84 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4G1B" FT BINDING 85 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /ligand_part_note="axial binding residue" FT /evidence="ECO:0007829|PDB:4G1B" FT BINDING 85 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /ligand_part_note="axial binding residue" FT /evidence="ECO:0007829|PDB:4G1V" FT BINDING 207 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V" FT BINDING 208 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V" FT BINDING 209 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4G1V" FT BINDING 210 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V" FT BINDING 223 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V" FT BINDING 225 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V" FT BINDING 230 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4G1V" FT BINDING 234 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V" FT BINDING 237 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V" FT BINDING 238 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V" FT BINDING 239 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4G1B, ECO:0007829|PDB:4G1V" FT BINDING 285 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0007829|PDB:4G1V" FT BINDING 393 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4G1V" FT BINDING 393 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4G1B" FT BINDING 394 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4G1V" FT BINDING 394 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4G1B" FT DISULFID 297 FT /note="Interchain" FT /evidence="ECO:0007829|PDB:4G1B" SQ SEQUENCE 399 AA; 44660 MW; 9AF1DE8280220D21 CRC64; MLAEKTRSII KATVPVLEQQ GTVITRTFYK NMLTEHTELL NIFNRTNQKV GAQPNALATT VLAAAKNIDD LSVLMDHVKQ IGHKHRALQI KPEHYPIVGE YLLKAIKEVL GDAATPEIIN AWGEAYQAIA DIFITVEKKM YEEALWPGWK PFEITAKEYV ASDIVEFTVK PKFGSGIELE SLPITPGQYI TVNTHPIRQE NQYDALRHYS LCSASTKNGL RFAVKMEAAR ENFPAGLVSE YLHKDAKVGD EIKLSAPAGD FAINKELIHQ NEVPLVLLSS GVGVTPLLAM LEEQVKCNPN RPIYWIQSSY DEKTQAFKKH VDELLAECAN VDKIIVHTDT EPLINAAFLK EKSPAHADVY TCGSLAFMQA MIGHLKELEH RDDMIHYEPF GPKMSTVQV //