ID A0A2T9XTF8_9CELL Unreviewed; 490 AA.
AC A0A2T9XTF8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=DDP54_10515 {ECO:0000313|EMBL:PVU83357.1};
OS Cellulomonas sp. WB94.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2173174 {ECO:0000313|EMBL:PVU83357.1, ECO:0000313|Proteomes:UP000245142};
RN [1] {ECO:0000313|EMBL:PVU83357.1, ECO:0000313|Proteomes:UP000245142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB94 {ECO:0000313|EMBL:PVU83357.1,
RC ECO:0000313|Proteomes:UP000245142};
RA Anderson E., Ishii S., Jang J.;
RT "Cellulomonas - woodchip bioreactor.";
RL Submitted (APR-2018) 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 -!- 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:PVU83357.1}.
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DR EMBL; QEES01000002; PVU83357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9XTF8; -.
DR OrthoDB; 833207at2; -.
DR Proteomes; UP000245142; 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:SF105; DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10668; PHYTOENE DEHYDROGENASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000245142}.
FT DOMAIN 19..253
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 490 AA; 50409 MW; 8E10A423C5E7D455 CRC64;
MSRARSTEVD AVVVGSGPGG LAAAVTLARA GLSVQVVEAQ DTIGGGSRTL DLGLADGVLH
DVCSAVHPLA VASPFLQSFD LEARGVEMLA AEAAYAQPLD GGRAAVAYRS IERTADALGP
DGPAWRRLLG PLSTHPDGLV DVALGDRRSM PRDLGTAVRF GLGVLEQGSV AWGARFRTEE
AAALLTGVAA HAIAPMPSLT AAGAAVMLAA LAHGPGWPIP RGGSQSIVDA LAADLRAHGG
SIVTGTEVHD LDELPRAQAY LFDTTPRTLV RVLGRRLPGR AARSFARFPA GNAAAKVDFV
LSGPVPWTRP EVGLAGTVHV GGSRAQMAAA EAAVAAGRHA EHPMVLLSDP TTADATRFGA
GGLRPLWTYA HVPNGSTLDL TDAVTRQVER FAPGFRDVVV AARCVPAAQM SEHNANYAGG
DIAGGAVSLY RMFARPRPVW DPFDGGLPGV YLCSASVPPG PGVHGLGGWY AATRALRSRF
GITQPPSLAP
//
