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Database: UniProt
Entry: A0A429VAB0_9SPHN
LinkDB: A0A429VAB0_9SPHN
Original site: A0A429VAB0_9SPHN 
ID   A0A429VAB0_9SPHN        Unreviewed;       527 AA.
AC   A0A429VAB0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 9.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   ORFNames=HMF7854_08440 {ECO:0000313|EMBL:RST30865.1};
OS   Sphingomonas ginkgonis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=2315330 {ECO:0000313|EMBL:RST30865.1, ECO:0000313|Proteomes:UP000274661};
RN   [1] {ECO:0000313|EMBL:RST30865.1, ECO:0000313|Proteomes:UP000274661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF7854 {ECO:0000313|EMBL:RST30865.1,
RC   ECO:0000313|Proteomes:UP000274661};
RA   Cha I., Kang H., Kim H., Kang J., Joh K.;
RT   "Sphingomonas sp. HMF7854 Genome sequencing and assembly.";
RL   Submitted (DEC-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:RST30865.1}.
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DR   EMBL; RWJF01000001; RST30865.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A429VAB0; -.
DR   OrthoDB; 9774675at2; -.
DR   Proteomes; UP000274661; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000274661}.
FT   DOMAIN          13..296
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   527 AA;  56297 MW;  C9CF46E04506B0D7 CRC64;
     MYDAVIIGAG HNGLTCAFYL ARKGLKVAVL EAQGTVGGAA VTDEFLPGFR NSAASYTVSL
     LQPRVIQDMD LARHGLKVVL RKIDNFLPGE NGYLLGGRNG LTRAELARHH PEDGPAYDRY
     TAELETVVPL IQKWLLKSPP QAGGGVRGLP TLLQLGKDLA GLKPDEIRTV HAYATKSAGD
     ILDRHFTGDL AKALFGFDGV VGNFASPYSP GTAYVLLHHL FGEAAGVPGA WGHAIGGMGA
     ITQAMARAAR EAGVDIVLGT PVEEVVVERG RAAGVVAGGK AWRAPTVIAN VNPRLLFERL
     MPAGAVAAPV ETHMKEWACE SATFRMNVAL SELPKFTVKP EAGDHLTAGI IIAPSLDYMD
     KAYLDARRDG WSKQPIVEML IPSTLDDTLA PKGKHVASLF CQHFRYNLPA GKNWDKVRDK
     VADQVIATVD HHAPGFAASV IGRQIHSPLD LERRFGLIGG DIFHGKMGLD QLFSARPMIG
     AADYRMPLKG LYLCGSGAHP GGGVTGAPGH NAAKAVLADR RPWRRRA
//
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