ID Q55808_SYNY3 Unreviewed; 542 AA.
AC Q55808;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN Name=crtO {ECO:0000313|EMBL:BAA10561.1};
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC Synechocystis.
OX NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA10561.1, ECO:0000313|Proteomes:UP000001425};
RN [1] {ECO:0000313|EMBL:BAA10561.1, ECO:0000313|Proteomes:UP000001425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa {ECO:0000313|Proteomes:UP000001425};
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA10561.1; -; Genomic_DNA.
DR PIR; S76617; S76617.
DR AlphaFoldDB; Q55808; -.
DR IntAct; Q55808; 1.
DR STRING; 1148.gene:10500065; -.
DR PaxDb; 1148-1001724; -.
DR EnsemblBacteria; BAA10561; BAA10561; BAA10561.
DR KEGG; syn:slr0088; -.
DR eggNOG; COG1233; Bacteria.
DR InParanoid; Q55808; -.
DR PhylomeDB; Q55808; -.
DR BioCyc; MetaCyc:MONOMER-19183; -.
DR BRENDA; 1.14.99.63; 6192.
DR BRENDA; 1.17.5.B2; 382.
DR BRENDA; 1.3.5.B4; 382.
DR Proteomes; UP000001425; 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; PHYTOENE DEHYDROGENASE; 1.
DR PANTHER; PTHR10668:SF103; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001425}.
FT DOMAIN 225..312
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 542 AA; 59400 MW; CD673A75E5CE7928 CRC64;
MITTDVVIIG AGHNGLVCAA YLLQRGLGVT LLEKREVPGG AATTEALMPE LSPQFRFNRC
AIDHEFIFLG PVLQELNLAQ YGLEYLFCDP SVFCPGLDGQ AFMSYRSLEK TCAHIATYSP
RDAEKYRQFV NYWTDLLNAV QPAFNAPPQA LLDLALNYGW ENLKSVLAIA GSKTKALDFI
RTMIGSPEDV LNEWFDSERV KAPLARLCSE IGAPPSQKGS SSGMMMVAMR HLEGIARPKG
GTGALTEALV KLVQAQGGKI LTDQTVKRVL VENNQAIGVE VANGEQYRAK KGVISNIDAR
RLFLQLVEPG ALAKVNQNLG ERLERRTVNN NEAILKIDCA LSGLPHFTAM AGPEDLTGTI
LIADSVRHVE EAHALIALGQ IPDANPSLYL DIPTVLDPTM APPGQHTLWI EFFAPYRIAG
LEGTGLMGTG WTDELKEKVA DRVIDKLTDY APNLKSLIIG RRVESPAELA QRLGSYNGNV
YHLDMSLDQM MFLRPLPEIA NYQTPIKNLY LTGAGTHPGG SISGMPGRNC ARVFLKQQRR
FW
//
