ID A1VLP8_POLNA Unreviewed; 463 AA.
AC A1VLP8;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Multicopper oxidase, type 3 {ECO:0000313|EMBL:ABM36576.1};
GN OrderedLocusNames=Pnap_1261 {ECO:0000313|EMBL:ABM36576.1};
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM36576.1, ECO:0000313|Proteomes:UP000000644};
RN [1] {ECO:0000313|Proteomes:UP000000644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644};
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(2009).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR EMBL; CP000529; ABM36576.1; -; Genomic_DNA.
DR RefSeq; WP_011800667.1; NC_008781.1.
DR AlphaFoldDB; A1VLP8; -.
DR STRING; 365044.Pnap_1261; -.
DR KEGG; pna:Pnap_1261; -.
DR eggNOG; COG2132; Bacteria.
DR HOGENOM; CLU_034184_0_0_4; -.
DR OrthoDB; 9757546at2; -.
DR Proteomes; UP000000644; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13860; CuRO_1_2dMco_1; 1.
DR CDD; cd04202; CuRO_D2_2dMcoN_like; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 2.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709:SF218; FI03373P-RELATED; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000644};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..463
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002639988"
FT DOMAIN 87..192
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 219..332
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 408..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 51059 MW; 30FA43F46049B4EF CRC64;
MNRRNFFNGA ALTAVAAASV NRVALAALPE PVLMTGADTA PPLVPSSGRP YNPVVTLNGW
TLPWRMNNGV KEFHLVAEPV VREMAPGFKA HMWGYNGQSP GPTIEVVEGD RVRVFVTNRL
PEHTSVHWHG QRLPNGMDGV SGLTQPSIGV GKTFVYEFVA RRPGTFMYHP HADEMTQMAM
GMMGFWVTHP KARHPLIDEV DRDFVFLLSA YDIDPGTMTP KIMTMTDFNL WTWNSRIFPG
IDTFNVRQGD KVRMRIGNLT MTNHPMHLHG HEFKVTGGDG GPWPLAARWP EVTTDVGVGQ
MRQLEFVADE EGDWAFHCHK SHHTMNAMGH AIPTTIGVDH RGLVGKLQKA MPDYMVMGER
GMADMGAMEM PIPENTAPMM TGTGPYGGVE MGGMFSVLKV RKDQKPGDYK DPGWFRQPPG
TRAFEWTGAL PDPARMKPSA ATPAPAGPQT EVQIRKPTGH AGH
//
