ID A0A2G8JHI9_STIJA Unreviewed; 458 AA.
AC A0A2G8JHI9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=BSL78_27969 {ECO:0000313|EMBL:PIK35212.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK35212.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK35212.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK35212.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK35212.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
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 -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006046}.
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:PIK35212.1}.
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DR EMBL; MRZV01001957; PIK35212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8JHI9; -.
DR STRING; 307972.A0A2G8JHI9; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000230750}.
FT DOMAIN 62..343
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 458 AA; 50117 MW; 76E83AC1D64C37D2 CRC64;
MKYPPFTVQK ILFGNKIRTV KSLGKPYWYL RLPWLQQCRP ASGGDPLTKD YDVIIVGAGH
NGLVASAYLQ MAGLQTLVLE RRHIIGGQQS QKKSFQKRGL KVYTRPHFAF TPLLEEPGQN
GRPRSLLLGK DHESTYQQIA KFLKKMQRCL NLVEVAFPEY EKYIAKLGEA IEPLLDMSPV
DIQSLTEGTL RKRLKALPAL RTLMQTGLAL GKDIPAFYEI LTAPAKKILD RWFDSEPLKA
TIATDAVIGA MLTPDQPGSG YVLLHHVMGQ IDGEKGAWGF VEGGMGSVSR CISEAALEHG
ATILTNKTVS SLLSDSDKKV CGVVLEDGTE IRSKAVLSNA TLSNGREWDE ETKKAYADIV
FDAVEQYAPG FKDSIVGADI LPPPELERIF GLTGGNIFHG ALSLDQLYLA RPYPWCSSYR
TPVKGLYLCG SGAHPGGGVM GAPGYNSAQI VKTDFAAM
//
