ID   E6PDG1_9ZZZZ            Unreviewed;       504 AA.
AC   E6PDG1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   ORFNames=CARN1_1598 {ECO:0000313|EMBL:CBH74496.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:CBH74496.1};
RN   [1] {ECO:0000313|EMBL:CBH74496.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F.,
RA   Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C.,
RA   Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O.,
RA   Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N.,
RA   Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P.,
RA   Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., Medigue C.,
RA   Le Paslier D.;
RT   "Diversity of trophic interactions inside an arsenic-rich microbial
RT   ecosystem.";
RL   Submitted (OCT-2009) 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   -!- 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:CBH74496.1}.
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DR   EMBL; CABL01000002; CBH74496.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6PDG1; -.
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   4: Predicted;
FT   DOMAIN          15..498
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   504 AA;  54091 MW;  BC5E72071178AF79 CRC64;
     METYDALVIG SGHNGLAAAA LLSDAGLRVA ILERSDRIGG ATVSERDRWP GYTISAASYV
     CSLLDPWLIE RLDLRAHGYD AYRKDPASFT PLLDGRSLLL GADEEQNAEE IARFDPADIA
     GFAAFDREAT ALGSALFERF ADMEPRFDRF DAQVRAALEG SVAALVERHV RTPVLQATLA
     TDGLIGTYRG PFDAGTGYVL AHHYAGRAFG VQGAWGFVRG GMGAISQALL SAAQARGARA
     FTDANVTRFL LDGDRVVGAV TADGREFRAH AVLSNAHPVT TYRDLLGEKH LDDATKGALA
     RWQSVGPALK LNLALGELPN FSARPGTTLQ PHHRATIHVA PDLAFLQRAH DDARRTGESE
     EPMLECFMQT PTDPSLAPPG KHILSIFAQY FPADRPGGWD TARRDGAVEK IVAQLARYAP
     NIPNAIEARQ LMVAPDLEER FGLIGGHIFH GELLPGQIYE GRFGVRSPIA GLYLCGSGTH
     PGGCVSGFPG RRAAQAVLAD RVLA
//