ID J5ENH0_9MYCO Unreviewed; 525 AA.
AC J5ENH0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=MCOL_V208945 {ECO:0000313|EMBL:EJO90304.1};
OS Mycobacterium colombiense CECT 3035.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1041522 {ECO:0000313|EMBL:EJO90304.1, ECO:0000313|Proteomes:UP000006455};
RN [1] {ECO:0000313|EMBL:EJO90304.1, ECO:0000313|Proteomes:UP000006455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 3035 {ECO:0000313|EMBL:EJO90304.1,
RC ECO:0000313|Proteomes:UP000006455};
RX PubMed=21952541; DOI=10.1128/JB.05928-11;
RA Gonzalez-Perez M., Murcia M.I., Landsman D., Jordan I.K.,
RA Marino-Ramirez L.;
RT "Genome sequence of the Mycobacterium colombiense type strain, CECT 3035.";
RL J. Bacteriol. 193:5866-5867(2011).
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:EJO90304.1}.
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DR EMBL; AFVW02000002; EJO90304.1; -; Genomic_DNA.
DR RefSeq; WP_007771225.1; NZ_CP020821.1.
DR AlphaFoldDB; J5ENH0; -.
DR STRING; 1041522.GCA_002105755_01278; -.
DR GeneID; 31527171; -.
DR eggNOG; COG1233; Bacteria.
DR OrthoDB; 9774675at2; -.
DR Proteomes; UP000006455; 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; 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;
FT DOMAIN 17..507
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 525 AA; 56743 MW; 640802CA44E8161A CRC64;
MTDTEYDAIV VGAGHNGLTA AAILQRAGLR TLCLEANTYA GGMAATVELI DGFRYEIAGS
VQFPLASQLT KDLGLDTLPA VEPDVMSVNI GEHGEEPMIF YRDPMRLMTH LSDRHGLEAV
TGMAELIGWS QGPAKALGRF DVRQAPKTFD EMYACAADDS ERRAIHEMLF GSAMDVIDRY
LPDKDKHAVM RGMLAFLAVN STYRGPYTPG SATCLAFALA VPQDDTAGTA MMTKLKGGIG
ALTEHLRELF IGHGGEIRFR TKAEEILVDR GKVTGVRLRD GSTISAPIVM SNLSPDVTLT
ELIAPEHVPA SLAARVCARD HRASFVQIHF ALDGLPEFAP PYEFLNTDGM QQSVGIFGSP
ESQQLHWENC RRGVVPDNPS MGMQIPSVHD PAMAPPGKHA ASAFAYAFPV ETSRDQHGHL
KNEMAQRVID KITRLAPNFK DIVIRHITFA PYHMNTMFGA PSGDFCHGLL HPDLMGPNRP
GPKGFLDMPI GIDGLYLAGA GCHGGPGITF TPGYNAAYQA LDDMA
//
