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Database: UniProt
Entry: H5WL82_9BURK
LinkDB: H5WL82_9BURK
Original site: H5WL82_9BURK 
ID   H5WL82_9BURK            Unreviewed;       542 AA.
AC   H5WL82;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   ORFNames=BurJ1DRAFT_1400 {ECO:0000313|EMBL:EHR70271.1};
OS   Burkholderiales bacterium JOSHI_001.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=864051 {ECO:0000313|EMBL:EHR70271.1, ECO:0000313|Proteomes:UP000004674};
RN   [1] {ECO:0000313|EMBL:EHR70271.1, ECO:0000313|Proteomes:UP000004674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JOSHI_001 {ECO:0000313|EMBL:EHR70271.1,
RC   ECO:0000313|Proteomes:UP000004674};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Zeytun A., Lu M., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Smith J., Lewis G.,
RA   Woyke T.;
RT   "Noncontiguous Finished sequence of Burkholderiales bacterium JOSHI_001.";
RL   Submitted (NOV-2011) 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}.
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DR   EMBL; CM001438; EHR70271.1; -; Genomic_DNA.
DR   AlphaFoldDB; H5WL82; -.
DR   STRING; 864051.BurJ1DRAFT_1400; -.
DR   eggNOG; COG1233; Bacteria.
DR   HOGENOM; CLU_019327_0_1_4; -.
DR   OrthoDB; 9774675at2; -.
DR   BioCyc; BBAC864051:G1H30-1390-MONOMER; -.
DR   Proteomes; UP000004674; Chromosome.
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   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000004674}.
FT   DOMAIN          15..321
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   542 AA;  58317 MW;  09F72B76B8304E83 CRC64;
     MSKRTAALIG GGHNGLVCAF YLARAGFDVT VFERRGVVGG AAVTESFHPG FRNSVASYTV
     SLLAPHIIAD MRLHERGLRI LERPLSNFLP LSDTQFLKLG GGLARTQAEV AKYSAKDAAA
     LPAYYARLDA MGDLLRELSR RTPPDLLSPS RSLPRAWAQA RLLNGLNAVQ KRDLLALFTQ
     SAAEFLDAWF ESDPVKTAFG FDAVVGHFDS PYSPGSAYVL LHHTFGGVNG KKGIWGHAVG
     GMGAITQAMA RACEAHGVVL RTDSPVARVQ VNQGRATGVQ LEDGSRFSAD LVAANVNPHL
     LFTRMVDAAD LPADFAQRMA HYKSHSGTLR MNVALSELPS FTCLPNTGPA LAEHHASGII
     MAPSLAYMDR AHQDARAFGW SRQPIVEMLI PSSVDDSLAP PGQHVASLFC QHFAYTLPDG
     QTWDDCREQA ADLVTDTVTR WAPNFKRSVL GRMVLTPLDL ERTFGLVGGD IFHGVMSLNQ
     MWAARPVLGH GDHRAPIAGL YLCGSGTHPG GGVSGLPGYN AAREIRRDHS AWAALKFALA
     GE
//
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