ID A0A061LZ06_9MICO Unreviewed; 523 AA.
AC A0A061LZ06;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=H490_0107450 {ECO:0000313|EMBL:EYT54724.1};
OS Leucobacter sp. UCD-THU.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1292023 {ECO:0000313|EMBL:EYT54724.1, ECO:0000313|Proteomes:UP000026917};
RN [1] {ECO:0000313|EMBL:EYT54724.1, ECO:0000313|Proteomes:UP000026917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-THU {ECO:0000313|EMBL:EYT54724.1,
RC ECO:0000313|Proteomes:UP000026917};
RX PubMed=23792744; DOI=10.1128/genomeA.00325-13;
RA Holland-Moritz H.E., Bevans D.R., Lang J.M., Darling A.E., Eisen J.A.,
RA Coil D.A.;
RT "Draft Genome Sequence of Leucobacter sp. Strain UCD-THU (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:S69-S82(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:EYT54724.1}.
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DR EMBL; APJM01000011; EYT54724.1; -; Genomic_DNA.
DR RefSeq; WP_017884143.1; NZ_KB714602.1.
DR AlphaFoldDB; A0A061LZ06; -.
DR STRING; 1292023.H490_0107450; -.
DR HOGENOM; CLU_019327_0_1_11; -.
DR Proteomes; UP000026917; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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:UP000026917}.
FT DOMAIN 14..451
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 523 AA; 56508 MW; 1CE2739CFE619718 CRC64;
MTSHVLVIGG GHNGLVAANY LAMTGHRVTL VEQRERLGGV VGRFEYMPGY ASSITNSPGS
FEGAIMQELR LQDFGLRFHR PETTLLHPMD DGLFVGWRDP QLVEEQMERM APGEFARHRE
LVSRLDRLGE QVGLSMWERP LDQRAVLERM DPGPRDEFRR SMIEGSLEEL LDEALRSDQV
KSLMMMLALN GQLLSPRAQG SAFGLMLRPI SRASGATDVL GIRDVPLRGS VGLPIGSMAA
IVDALEAAAR AHGVAIRTGS GVAELQFDDS GRVSAAVLES GESVEQLDAV VSTVETSRLH
RMIPDDTIPE SAWPPAPDGS AFKIALALDG LPSVAGAPVG VPEEVLLSTQ FRIGPNPGYI
ADAVEQGIAG RPSDKPIIWG LIPSLTSPGL APEGRHLMSL NVWHAPHRLG ERYWRENGAA
FADRCVAQVE AAFPGLSERI TDRRWLGPHD LEREFGLTSS NITHGDLTPE SMLNGRPGAE
LSAGLERRGI VLGGAESWPG GYVTGAPGRR AALTIARKKE PTR
//
