ID A0A0R2UIJ8_9GAMM Unreviewed; 525 AA.
AC A0A0R2UIJ8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=ABS24_10695 {ECO:0000313|EMBL:KRO97037.1};
OS SAR92 bacterium BACL26 MAG-121220-bin70.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Porticoccaceae; SAR92 clade.
OX NCBI_TaxID=1655626 {ECO:0000313|EMBL:KRO97037.1, ECO:0000313|Proteomes:UP000051213};
RN [1] {ECO:0000313|EMBL:KRO97037.1, ECO:0000313|Proteomes:UP000051213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL26 MAG-121220-bin70 {ECO:0000313|EMBL:KRO97037.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) 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:KRO97037.1}.
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DR EMBL; LICA01000021; KRO97037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2UIJ8; -.
DR Proteomes; UP000051213; Unassembled WGS sequence.
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 19..519
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 525 AA; 56302 MW; C89E2A54C60BB5B6 CRC64;
MIDLTKNYDV IVVGGGHNGL ICATYLAKSG RKVLVIEANQ SLGGASATSE FSDQFSVSSC
AQWLFQLNPV VASDMGLKKQ GLELAARDLN TIALAEDGNH LIIDGDKLEG AGISDEDRIA
FVAFNKQILR FAKLLSGAFN RRAPKLVESN LTDRITLAKL GLGMKMLGKD DMSDLMRLAL
INIYDVMEEN FDNELLKAAI SLDSLLGSHM GPRSPNTVYG YFYRRMGDIF GFSGPAVVKG
GMGAVGEAMA KAARASGVDI EVGTAVSKIN IAIDRVTGVT LADGRVVDAG LVVSNADPKT
TFNKLVGLTN IETGVARRVK SMRMKGDAAK LHIALDSLPS FTGLSEQQMG QRLLIAPSMN
YIEKAFNHSK YGEYSTAPAM DISIPTIHDS SLAPAGKHVM SVIVQFAPYE LNGGWDDENK
EEFKRLVIDR IADYAPDLKD KIIASELLTP SDIEARFHIQ GGHWHHGEIS LDQILTMRPF
PGASQYGTSV DGLFLCGAGT HPGGGVMGLA GHNAAKEIIK RGKSA
//