ID I1MNG0_SOYBN Unreviewed; 565 AA.
AC I1MNG0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN Name=100781247 {ECO:0000313|EnsemblPlants:KRH08274};
GN ORFNames=GLYMA_16G139600 {ECO:0000313|EMBL:KRH08274.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH08274.1};
RN [1] {ECO:0000313|EMBL:KRH08274.1, ECO:0000313|EnsemblPlants:KRH08274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH08274};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH08274.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH08274}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH08274};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH08274.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH08274.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable oxidoreductase that may play a role as regulator of
CC mitochondrial function. {ECO:0000256|ARBA:ARBA00037217}.
CC -!- SUBUNIT: Interacts with COX5B; this interaction may contribute to
CC localize PYROXD2 to the inner face of the inner mitochondrial membrane.
CC {ECO:0000256|ARBA:ARBA00038825}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006046}.
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DR EMBL; CM000849; KRH08274.1; -; Genomic_DNA.
DR RefSeq; XP_003547987.1; XM_003547939.3.
DR AlphaFoldDB; I1MNG0; -.
DR SMR; I1MNG0; -.
DR STRING; 3847.I1MNG0; -.
DR PaxDb; 3847-GLYMA16G25390-1; -.
DR EnsemblPlants; KRH08274; KRH08274; GLYMA_16G139600.
DR GeneID; 100781247; -.
DR Gramene; KRH08274; KRH08274; GLYMA_16G139600.
DR KEGG; gmx:100781247; -.
DR eggNOG; KOG4254; Eukaryota.
DR HOGENOM; CLU_019327_0_1_1; -.
DR InParanoid; I1MNG0; -.
DR OMA; GLYHCGS; -.
DR OrthoDB; 179056at2759; -.
DR Proteomes; UP000008827; Chromosome 16.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10668; PHYTOENE DEHYDROGENASE; 1.
DR PANTHER; PTHR10668:SF103; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT DOMAIN 33..366
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 565 AA; 61377 MW; B2BA8C1C67FF8C7C CRC64;
MWRRSFSSST AATTATLKGK KWDALIIGGG HNGLTAAAYL ARGGLSVAVL ERRHVIGGAA
VTEELVPGFK FSRCSYLQSL LRPSVIKELE LGKHGLKLLK RNPSSFTPCL DGRYLLLGPD
KDLNHSEISK FSLADAQAYP RYESQLESFC KFMDLVLDSP PPESVHHKSS INEKLKNKIQ
NSVFWASCLR QVSSLGQKDM VNFMDLLLSP ASKVLNNWFE TDVLKATLAT DAVIGSTASV
HTPGSGYVLL HHVMGETDGE RGIWSYVEGG MGSISKAIGN AAIEAGAHVV TNAEVSRLLI
ENTSTVCGVT LADGTEVHSS IVLSNATPYK TFMELVPNDI LPDDFVRAIK HSDYSSATTK
LNVAVDKLPE FRCCKLDHPH AGPQHVGTIH IGSESMEEIH SACQDAVNGV PSRRPVIEMT
IPSVLDKTIS PPGKHVINLF VQYTPYKPLD GDWQDHDYRE SFAQKCFKLI DEYAPGFSTS
IIGYDMLTPP DLEREIGLTG GNIFHGAMGL DSLFLMRPAK GWSNYKTPLR GLYLCGSGAH
PGGGVMGAPG RNAARLVLQE VGERT
//
