ID A3KJ36_STRA7 Unreviewed; 539 AA.
AC A3KJ36;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=SAM23877_0815 {ECO:0000313|EMBL:AKZ53864.1}, SAML0734
GN {ECO:0000313|EMBL:CAJ89720.1};
OS Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 /
OS NBRC 12836 / NRRL B-2516).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=278992 {ECO:0000313|EMBL:CAJ89720.1};
RN [1] {ECO:0000313|EMBL:CAJ89720.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 23877 {ECO:0000313|EMBL:CAJ89720.1};
RX PubMed=16956972; DOI=10.1093/molbev/msl108;
RA Choulet F., Aigle B., Gallois A., Mangenot S., Gerbaud C., Truong C.,
RA Francou F.X., Fourrier C., Guerineau M., Decaris B., Barbe V.,
RA Pernodet J.L., Leblond P.;
RT "Evolution of the terminal regions of the Streptomyces linear chromosome.";
RL Mol. Biol. Evol. 23:2361-2369(2006).
RN [2] {ECO:0000313|Proteomes:UP000061018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL
RC B-2516 {ECO:0000313|Proteomes:UP000061018};
RX PubMed=26410452; DOI=10.1016/j.jbiotec.2015.09.020;
RA Thibessard A., Haas D., Gerbaud C., Aigle B., Lautru S., Pernodet J.L.,
RA Leblond P.;
RT "Complete genome sequence of Streptomyces ambofaciens ATCC 23877, the
RT spiramycin producer.";
RL J. Biotechnol. 214:117-118(2015).
RN [3] {ECO:0000313|EMBL:AKZ53864.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23877 {ECO:0000313|EMBL:AKZ53864.1};
RA Thibessard A., Haas D., Gerbaud C., Aigle B., Lautru S., Pernodet J.-L.,
RA Leblond P.;
RT "Complete genome sequence of Streptomyces ambofaciens ATCC 23877, the
RT spiramycin producer.";
RL Submitted (JUL-2015) 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; CP012382; AKZ53864.1; -; Genomic_DNA.
DR EMBL; AM238663; CAJ89720.1; -; Genomic_DNA.
DR RefSeq; WP_053126845.1; NZ_CP012382.1.
DR AlphaFoldDB; A3KJ36; -.
DR STRING; 1889.SAM40697_0697; -.
DR KEGG; samb:SAM23877_0815; -.
DR Proteomes; UP000061018; 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:SF105; DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10668; PHYTOENE DEHYDROGENASE; 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:UP000061018}.
FT DOMAIN 13..504
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 539 AA; 57381 MW; 1296E1FF33195D9B CRC64;
MPDAVVIGSG PNGLVAANLL VDAGWSVEVL EEQPEPGGAV RHDSEVAPGF VNDLFSSFYP
LAAASPVLAG LRLQDHGLRW GHAPHVLAHP LTDGTCAVLD RDVATTAASL DAFAPGDGAA
WDRLHEVWDR YRADILDALF TPFPPVRAGA RLALRLRGGG GLRLARTLVL PVRRMGEEEF
RGEGGKLILA GNALHADLAP EAAGSGGFGW LMSMLGQTYG FPVPVGGSGA LTAALVHRLR
ARGGTLRCGQ RVEQVLVRDR RVTGVRTAGG ETVTARRAVL ADVSVPALYG GLVAPEHLPD
QVLADLRRFQ WDFATFKVDW ALDGPVPWRC EDAARAGTVH LADGLDELTR FAAQIAMRQV
PDRPFSLFGQ MTTTDPSRSP SGTESAWAYT HVPHDIRADA GDEGITGSWD AREQELMADR
VERQVERFAP GFRGLIRARR VLAPPTLQAM NANLEGGAIN GGTTAMHQQL VFRPVPGTGR
PETPVTGLFL ASAGAHPGGG VHGAPGANAA RAALRQHRFA GLARAQRALT RRDRIGDKR
//