ID D3PZK0_STANL Unreviewed; 534 AA.
AC D3PZK0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN OrderedLocusNames=Snas_1978 {ECO:0000313|EMBL:ADD41674.1};
OS Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS NBRC 102104 / LLR-40K-21).
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Stackebrandtia.
OX NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD41674.1, ECO:0000313|Proteomes:UP000000844};
RN [1] {ECO:0000313|EMBL:ADD41674.1, ECO:0000313|Proteomes:UP000000844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX PubMed=21304662; DOI=10.4056/sigs.47643;
RA Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT 40K-21).";
RL Stand. Genomic Sci. 1:292-299(2009).
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; CP001778; ADD41674.1; -; Genomic_DNA.
DR RefSeq; WP_013017245.1; NC_013947.1.
DR AlphaFoldDB; D3PZK0; -.
DR STRING; 446470.Snas_1978; -.
DR KEGG; sna:Snas_1978; -.
DR eggNOG; COG1233; Bacteria.
DR HOGENOM; CLU_019327_0_1_11; -.
DR OrthoDB; 9774675at2; -.
DR Proteomes; UP000000844; 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 SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000844}.
FT DOMAIN 16..512
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 534 AA; 57622 MW; A3BD62875DAE0E1E CRC64;
MDGDFDVIVV GGGHNGLVAA AYLAKAGLKV CVCEAREVVG GAAVSEHPFG PQYTVTSLSY
VVSLLPQDLV TDLNLKEHGY HVYPQGPYFA PRREGGYLSL PEDPKERHAK IAEFSARDAD
AYEEWDAWLS QLGGLLGPLL ERIPPKLGSR RPMDLVRQAG LLKQLRGIDT RAAVDITRIM
TDSIADLIEE RFESEALRGL LAVSGCIGTW AGPRSAGTAY VMLHHHIGDI GDGNTGAWGF
PRGGMGGVTQ ALARSARQFG ATIRTASRVA RINVDNGRAI GVTLDNGDEL RAATTITTAH
PRVTFTDLID AGELPDDFLA DINRWKTRSG TVKINLAVDK LPTFTSHPEF DPWVHGGTIV
LAESLDDIEN AYQQAVSGKP AEFPFADVCI PSVFDDSLAP EGHHVVSMFT QWVPHTWASE
PDAEGLSDYA NRAVARMEAI APGFTDSIID FQVIGPHEME TEYGLVGGNI FHGELTPGQL
FHARPAAGFA DLRTPLKGLY QAGSSTHGGG GVTGIPGRNV VRQILADRRR PWRR
//
