ID B4WIP1_SYNS7 Unreviewed; 558 AA.
AC B4WIP1;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=S7335_3560 {ECO:0000313|EMBL:EDX85857.1};
OS Synechococcus sp. (strain ATCC 29403 / PCC 7335).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=91464 {ECO:0000313|EMBL:EDX85857.1, ECO:0000313|Proteomes:UP000005766};
RN [1] {ECO:0000313|EMBL:EDX85857.1, ECO:0000313|Proteomes:UP000005766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29403 / PCC 7335 {ECO:0000313|Proteomes:UP000005766};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS989904; EDX85857.1; -; Genomic_DNA.
DR RefSeq; WP_006455611.1; NZ_DS989904.1.
DR AlphaFoldDB; B4WIP1; -.
DR STRING; 91464.S7335_3560; -.
DR eggNOG; COG1233; Bacteria.
DR HOGENOM; CLU_019327_0_1_3; -.
DR OrthoDB; 544714at2; -.
DR Proteomes; UP000005766; 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 PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000005766}.
FT DOMAIN 15..298
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 558 AA; 62052 MW; 50A04C4FDF6AE141 CRC64;
MENYDVVIIG AGHNGLVCAA YLLKAGYSVA LLEKRSIPGG AATTEELMPE EAPGFMFNRC
AIDHEFIHLG PVIEELELHK YGLEYLFCDP TVFCPHPDGK YFLSYKSVDK TCEEIAQFSR
RDAEKYREFI DFWQRFTKAI QPVFNAPPQA IFDILGNYDI KSIQNLLSIL GGPHKSLDLI
RTMLTSPKDL LDEYFDSEFL KAPLSRLASE FGAPPSQKTI SVGGMMMSMR HNPGMARPKG
GTGALIQALL KLVKAQGGVV LTEQNVKRIL VDGKRAVGVE VQNGTEYRAK HGVISNIDAK
RVFLQLLESE DVAAVDKDLQ ERLDRRIVNN NETILRIDCA LSEVPRFEHH NHRDEYLVGS
VLIADSVRHV EIAHQEPEVG NIPDADPSFY AVVPTVRDPS MAPDGRHTLW VEFFAPYQIN
GAEGTGFAGT GWTDELKNQV ADRVIDKLAD YAPNIKQSII ARNVESPAEL GDRLGAYKGN
YYHVDMTLDQ MVFFRPLPEI ANYTTPFDGL FLTGAGTHPG GAISGMPGRN CARTFLNQQQ
PVLNRIREIG KTVFPKLS
//