ID Q1QJS4_NITHX Unreviewed; 535 AA.
AC Q1QJS4;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN OrderedLocusNames=Nham_2744 {ECO:0000313|EMBL:ABE63523.1};
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=323097 {ECO:0000313|EMBL:ABE63523.1, ECO:0000313|Proteomes:UP000001953};
RN [1] {ECO:0000313|EMBL:ABE63523.1, ECO:0000313|Proteomes:UP000001953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10229 / NCIMB 13809 / X14
RC {ECO:0000313|Proteomes:UP000001953};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA Gentry M.E., Bruce D., Richardson P.;
RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL Submitted (MAR-2006) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000319; ABE63523.1; -; Genomic_DNA.
DR RefSeq; WP_011511189.1; NC_007964.1.
DR AlphaFoldDB; Q1QJS4; -.
DR STRING; 323097.Nham_2744; -.
DR KEGG; nha:Nham_2744; -.
DR eggNOG; COG1233; Bacteria.
DR HOGENOM; CLU_019327_0_1_5; -.
DR OMA; GLYHCGS; -.
DR OrthoDB; 9774675at2; -.
DR Proteomes; UP000001953; 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 SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001953}.
FT DOMAIN 15..322
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 535 AA; 56863 MW; 5C26CD5A3B8B4046 CRC64;
MSDTDVVIIG AGHNGLTCAA YLAMAGLRVK VVERRKVVGG AAVTEEFQPG FRNSVAAYTV
SLLNPKVIAD LRLHDHGLRI VERRAQNFLP APDGRYLLTG EGRTAASVAG LSERDAGALG
GFMRELEEIA DVIRQFVLRA PPNLVEGFGL NAAHEIVNAI GSAGILRGLS LEQQRSLLDL
FTRSAGDMLD DRFEIDLVKA LFGFDAIVGN YASPYAAGSA YVMLHHAFGE VNGKKGVWGH
AIGGMGAITQ AMAAAARARG AEIETDAGVC EVIVERGRAA GVVLDDGRTI RAKYVAANVN
PKLLYTRLLP AGALPAAFLN RIKTWRNGSG TFRMNVALEA LPSFSALPGA GDHLSAGIII
APGLGYMDRA WQDARQFGWS REPVVEVLIP SVIDDSLAPS GRHVASLFCQ HVAPQLPDGA
SWDDHRDEVA DLMIATVDLY APGFAASVIG RQILSPLDLE REFGLLGGDI FHGALTLNQL
FSARPMLGHA DYRGPLKGLY HCGSGAHPGG GVTGAPGHNA ARTILRDHRA LFARR
//