ID K9XQH9_STAC7 Unreviewed; 557 AA.
AC K9XQH9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN OrderedLocusNames=Sta7437_0753 {ECO:0000313|EMBL:AFZ34344.1};
OS Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC Stanieria.
OX NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ34344.1, ECO:0000313|Proteomes:UP000010473};
RN [1] {ECO:0000313|Proteomes:UP000010473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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}.
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DR EMBL; CP003653; AFZ34344.1; -; Genomic_DNA.
DR RefSeq; WP_015192017.1; NC_019748.1.
DR AlphaFoldDB; K9XQH9; -.
DR STRING; 111780.Sta7437_0753; -.
DR KEGG; scs:Sta7437_0753; -.
DR PATRIC; fig|111780.3.peg.786; -.
DR eggNOG; COG1233; Bacteria.
DR HOGENOM; CLU_019327_0_1_3; -.
DR OrthoDB; 9814556at2; -.
DR Proteomes; UP000010473; Chromosome.
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; 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:UP000010473}.
FT DOMAIN 15..518
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 557 AA; 61307 MW; FFEB3EADFC9925F0 CRC64;
METYDVIIIG AGHNGLVCAA YLLKAGYKVL LLEKRPVPGG AATTEEALPE QAPGFKFNLC
AIDHEFIFFS PIIEELQLTR YGLKYLSCDP HTFCPHPDGK YFLAHQSLEK TCAAIARYSA
RDAEKYREFV EYWTHLMGAI APWFNAPPQS VLAIARNYSQ KNLLDALKMV GSKNKALNFI
RTMITSPEDL LNQWFDTEIV KAPLARLAAE IGAAPSQKGI TAGLMMLAMR HHPGMARPQG
GTGALTQALV KLVTALGGVI LTEQMVKEVI VDDNRAVGVK VTGGKEYRAT KGVISNIDVQ
RLFLQLIEPG VVETELREKV QRNIVNNNET ILKIDCALSE PPRFEAYEHQ DEYLIGTILI
ADSVAHVEQA HSLAMMGQIP DQNPSMYLDV PSVLDPTLAP PGKHTLWIEF FAPYQIAGKE
GTGLNGTGWT DELKNQVADR VIDKLAQYAP NLKSSVIARR VESPAELGER LGSYKGNYYH
LDMTLDQMIF LRPLPEIANY TTPIKNLYLT GAGTHPGGSI SGMPGRNCAR VFLQQQSPIA
KAQQSILSVF NSVFAQA
//
