ID A0A016V084_9BILA Unreviewed; 527 AA.
AC A0A016V084;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN Name=Acey_s0020.g192 {ECO:0000313|EMBL:EYC21034.1};
GN Synonyms=Acey-F37C4.6 {ECO:0000313|EMBL:EYC21034.1};
GN ORFNames=Y032_0020g192 {ECO:0000313|EMBL:EYC21034.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC21034.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYC21034.1}.
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DR EMBL; JARK01001356; EYC21034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016V084; -.
DR Proteomes; UP000024635; 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 Pfam; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT DOMAIN 231..336
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 527 AA; 58497 MW; 9EB6BCC8AC9A40C5 CRC64;
MEYYSNKYLN NRAAYLARAG KRVCVLERRE VIGGAAVTEE IIPGFKFSRA SYLLSLLRPT
VIKDLNLKEH GLRYHIRNPY SFTPIRNSNE SLLLGHSVQE NCCEIAKFSK RDAEMFPKYE
DFIERIVRPL ESMMDEVPVN VRQSSKWKLL NKSWPLLRRV QQMGIANVVD FYELMTAPIA
KIMNRWFESD VLKATIGTDG VIGFAASPYD SGTGYVLLHH VLGGVDNRSG AWAYVIGGMG
AVSEAIAKSA RIHGAEIFVE QEVADILVDD GAVQGVRLAN GKEIHARTVL SNATPRVTFE
DLIAESHLTK EFLNAVKSID YTSPVTKINV AVRELPSFSC RPNAGASPMP HHQTTIHLNC
ESMEVVDEAV RDYRSGLWSR RPVIEMTIPS AVDRSLVPDN TSHVMSLFTQ YTPYQLRTGS
WDAELKEKYA KHVFNEIDAY APNFSLSVIG YEVLPPPDIE RIFGLTGGNI FHGSMSLDQL
YFTRPTSRYS NYTTPIKGLF LCGSGAHPGG GVTGAPGRLG ALAALQG
//
