ID Q82NN7_STRAW Unreviewed; 533 AA.
AC Q82NN7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 97.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=SAVERM_1264 {ECO:0000313|EMBL:BAC68974.1};
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC68974.1, ECO:0000313|Proteomes:UP000000428};
RN [1] {ECO:0000313|EMBL:BAC68974.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2] {ECO:0000313|EMBL:BAC68974.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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}.
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DR EMBL; BA000030; BAC68974.1; -; Genomic_DNA.
DR AlphaFoldDB; Q82NN7; -.
DR KEGG; sma:SAVERM_1264; -.
DR eggNOG; COG1233; Bacteria.
DR HOGENOM; CLU_019327_0_1_11; -.
DR OMA; GLYHCGS; -.
DR Proteomes; UP000000428; Chromosome.
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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000428}.
FT DOMAIN 28..315
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 533 AA; 56855 MW; 27ED9B735DD8FD0D CRC64;
MLPRTMAADE GHVPGRFDAV IVGGGHNGLV AAAYLARAGR SVLVLERLGN TGGAAVSTRP
FAGVDARLSR YSYLVSLLPR KIVRDLGLDF RVRGRTVSSY TPAERHGRPT GLLVGGGERR
TREAFGRLTG SAREYESWQR FYGMTGRVAR QVFPTLTEPL PSRDELRRRV DDEDAWRVLF
EEPIGAAIEE NFTDDLVRGV VLTDALIGTF ADAHDPSLRQ NRCFLYHIIG GGTGAWDVPV
GGMGALTDAL AAAARDAGAV LATGHEAVRI ETDGRSAEVT YRDADGEGTV SARHVLVNAA
PQELARLTGD SPPVPAEGAQ LKVNMLLKRL PALRDTAVDP REAFAGTFHI AEGYEQLAAA
HAQAAAGSLP EAPPSEIYCH SLTDPTILGP DLVEQGYQTL TLFGLHTPAR LFERDNEGVR
EELLKSTLAQ LDAHLAEPLV DCLATDAEGR PCIEAKSPLD LERDLRLPGG NIFHRDLAFP
YAQEGTGRWG VETAHANVLL CGAGAVRGGG VSGVPGHNAA MAALEDVGER ALG
//