ID A0A1B7M2V2_9MICC Unreviewed; 487 AA.
AC A0A1B7M2V2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=A6F49_04330 {ECO:0000313|EMBL:OAV62890.1};
OS Enteractinococcus helveticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae.
OX NCBI_TaxID=1837282 {ECO:0000313|EMBL:OAV62890.1, ECO:0000313|Proteomes:UP000078292};
RN [1] {ECO:0000313|EMBL:OAV62890.1, ECO:0000313|Proteomes:UP000078292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UASWS1574 {ECO:0000313|EMBL:OAV62890.1,
RC ECO:0000313|Proteomes:UP000078292};
RA Crovadore J., Chablais R., Lefort F.;
RT "First whole genome shotgun sequence of the bacterium Enteractinococcus sp.
RT strain UASWS1574.";
RL Submitted (APR-2016) 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:OAV62890.1}.
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DR EMBL; LXEY01000007; OAV62890.1; -; Genomic_DNA.
DR RefSeq; WP_043056053.1; NZ_LXEY01000007.1.
DR AlphaFoldDB; A0A1B7M2V2; -.
DR STRING; 1837282.A6F49_04330; -.
DR OrthoDB; 833207at2; -.
DR Proteomes; UP000078292; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.90.660.50; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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 PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
FT DOMAIN 18..470
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 487 AA; 52962 MW; 3E07E4933E121CDE CRC64;
MSETARPHVN IVGSGPNGLT AAAMLGRAGW RVRIFERNEI VGGAAASTDV FGDGSIVDLG
AAAHPFGVAS PVFRHLGLEE YGLKWLHSKY PMAHPFDDRP AAILHRDVRE TARALGVDST
AWRLIHRSLV NSIDDYLEQI MRPLLRFPNR PMKMARFGVL GTPPSSWFVR TAFREEAARA
LFTGSAAHAN TPLGHPFTST YGVLFSALGM TRGWPVIQGG TGALIDALVK LISEYDSEIH
TNYEVTDLDA LPAAQATILD ITPSQALVMR GKQLRELPDA TVQRFQRWRY GPGVYKVDWQ
LDGPVPWADS RVASATTVHV GGRAAEIRLA EAQVNAGRIP ERPFVMVVQP QVADPSRAPD
GKHILWTYTH VPHGYKPATK DREYVADVIQ SQIERFAPGF GTKVLAKKIW DPAALEEWNP
NLVGGDIAGG SMAGLQSLLR GGLTLEPYRT GVRGLYMCSS STPPGAGVHG MPGAWAAHAV
LEDQRNL
//
