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Database: UniProt
Entry: A0A0M2CQI6_9MICC
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Original site: A0A0M2CQI6_9MICC 
ID   A0A0M2CQI6_9MICC        Unreviewed;       480 AA.
AC   A0A0M2CQI6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   ORFNames=H488_0116635 {ECO:0000313|EMBL:EYT47959.1};
OS   Kocuria sp. UCD-OTCP.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1292021 {ECO:0000313|EMBL:EYT47959.1, ECO:0000313|Proteomes:UP000033173};
RN   [1] {ECO:0000313|EMBL:EYT47959.1, ECO:0000313|Proteomes:UP000033173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-OTCP {ECO:0000313|EMBL:EYT47959.1,
RC   ECO:0000313|Proteomes:UP000033173};
RX   PubMed=23661474;
RA   Coil D.A., Doctor J.I., Lang J.M., Darling A.E., Eisen J.A.;
RT   "Draft Genome Sequence of Kocuria sp. Strain UCD-OTCP (Phylum
RT   Actinobacteria).";
RL   Genome Announc. 1:E00172-13(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}.
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:EYT47959.1}.
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DR   EMBL; AOSQ01000045; EYT47959.1; -; Genomic_DNA.
DR   RefSeq; WP_017834389.1; NZ_AOSQ01000045.1.
DR   AlphaFoldDB; A0A0M2CQI6; -.
DR   HOGENOM; CLU_019327_1_1_11; -.
DR   Proteomes; UP000033173; 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; 2.
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          14..468
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   480 AA;  49995 MW;  9DD6C4DE85A7A660 CRC64;
     MQGTAAVVGS GPNGLAAAVV LARAGLDVTV HEAAGSAGGA ARSAAVLGPG TVVDLGSAVH
     PFGVASPLFA QLGLHRHGLE WLHPPVVAAH PLDDGPPGLL HRSLERTAAG LGADGRAWSL
     LHRGVVERWE ETVESVLGPL VRVPEHPRAL ASFGLRAPWP AAATARALFR TEQARGLFAG
     SAAHAVLPPR HALTSAFGTL FGAAAHATGW PVARGGTQAV VDALVADLEE HGGRVLVHSP
     VTDLAQVRPA DAVLLDLTPR QVLGLRGLEL PDRYRRALAR WRYGTASYKV DLLLDGPVPW
     RDPRVAEAGT VHVGGTLAEI GAAEQQARAG RLPERPFVLV AQQGAADPSR APAGRQVLWA
     YAHVPHGCDD PRAGERVLRQ LERFAPGVRD RIRERVDTSP AGLEAWNANL VGGDIGGGSL
     DGLQQLFRPA VQADPYATGV PGVWLCSSST PPGGGVHGMA GYHAARRALR GLARSRRPAG
//
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