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Database: UniProt
Entry: S4XX30_SORCE
LinkDB: S4XX30_SORCE
Original site: S4XX30_SORCE 
ID   S4XX30_SORCE            Unreviewed;       497 AA.
AC   S4XX30;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   ORFNames=SCE1572_22665 {ECO:0000313|EMBL:AGP37049.1};
OS   Sorangium cellulosum So0157-2.
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX   NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP37049.1, ECO:0000313|Proteomes:UP000014803};
RN   [1] {ECO:0000313|EMBL:AGP37049.1, ECO:0000313|Proteomes:UP000014803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So0157-2 {ECO:0000313|EMBL:AGP37049.1,
RC   ECO:0000313|Proteomes:UP000014803};
RX   PubMed=23812535; DOI=10.1038/srep02101;
RA   Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA   Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT   "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT   milieu.";
RL   Sci. Rep. 3:2101-2101(2013).
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; CP003969; AGP37049.1; -; Genomic_DNA.
DR   AlphaFoldDB; S4XX30; -.
DR   STRING; 1254432.SCE1572_22665; -.
DR   KEGG; scu:SCE1572_22665; -.
DR   PATRIC; fig|1254432.3.peg.5129; -.
DR   eggNOG; COG1233; Bacteria.
DR   HOGENOM; CLU_019327_1_1_7; -.
DR   Proteomes; UP000014803; 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:SF105; DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR10668; PHYTOENE DEHYDROGENASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
FT   DOMAIN          10..483
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   497 AA;  52957 MW;  AB9C9575E1FB38D8 CRC64;
     MIVVGSGPNG LTAAAYLARA GLSVLVLEAE QEPGGAVRTR EVTLPGFRHD LGAAFFPFGQ
     TSPALLPLDL PGAGLVWRHA PIDSAHPAPD GTCAAIARDV ETTARSLGED GPTWRRIAGW
     HAATVERLLK ALLSTPPALG ALLRFGPLNL LRLAQVALSS GRGFSTRTFR TEAARRVVPG
     LALHTDVGPE DPCGAIVGFM LTLLASSGGF AVPEGGAGSV TRALLRRIEE RSGSLRCGAR
     VAQIIARQGR AAAVRLADGE EIRARRAIVA DVAAPTLYLR LLAPELVPGR VQRAMRRFRQ
     GFGTFKMDWA LDGPAPWSHE DAARAAVVHA GDSLEDLAEF TRQVRAGVLP EHPYLVIGQQ
     SLVDPTRAPA GRHTLYAYSR VPSSIDGGWA ASRERFADRV EARIEELAPG FRQRILARKI
     WAPDDLEAMD ANLIGGDLGG GSADIRNQLI FRPVFPYFRY RTPLRGLYLG SSYAHPGAGV
     HGACGHNAAL AVLEDEG
//
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