GenomeNet

Database: UniProt
Entry: R4Z731_9ACTN
LinkDB: R4Z731_9ACTN
Original site: R4Z731_9ACTN 
ID   R4Z731_9ACTN            Unreviewed;       506 AA.
AC   R4Z731;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Putative Nitrite reductase (NO-forming) {ECO:0000313|EMBL:CCM65846.1};
DE            EC=1.7.2.1 {ECO:0000313|EMBL:CCM65846.1};
GN   ORFNames=BN381_80376 {ECO:0000313|EMBL:CCM65846.1};
OS   Candidatus Microthrix parvicella RN1.
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Microthrixaceae; Microthrix.
OX   NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM65846.1, ECO:0000313|Proteomes:UP000018291};
RN   [1] {ECO:0000313|EMBL:CCM65846.1, ECO:0000313|Proteomes:UP000018291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN1 {ECO:0000313|EMBL:CCM65846.1,
RC   ECO:0000313|Proteomes:UP000018291};
RX   PubMed=23446830; DOI=10.1038/ismej.2013.6;
RA   Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S.,
RA   Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., Nielsen P.H.;
RT   "Metabolic model for the filamentous 'Candidatus Microthrix parvicella'
RT   based on genomic and metagenomic analyses.";
RL   ISME J. 7:1161-1172(2013).
CC   -!- COFACTOR:
CC       Name=Cu(+); Xref=ChEBI:CHEBI:49552;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601287-1};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|PIRSR:PIRSR601287-1};
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:CCM65846.1}.
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; CANL01000078; CCM65846.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4Z731; -.
DR   STRING; 1229780.BN381_80376; -.
DR   eggNOG; COG2132; Bacteria.
DR   eggNOG; COG3794; Bacteria.
DR   HOGENOM; CLU_031740_1_2_11; -.
DR   OrthoDB; 345021at2; -.
DR   Proteomes; UP000018291; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd13921; Amicyanin; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR   InterPro; IPR035668; Amicyanin.
DR   InterPro; IPR000923; BlueCu_1.
DR   InterPro; IPR028871; BlueCu_1_BS.
DR   InterPro; IPR011706; Cu-oxidase_C.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR001287; NO2-reductase_Cu.
DR   PANTHER; PTHR36507; BLL1555 PROTEIN; 1.
DR   PANTHER; PTHR36507:SF1; CELL SURFACE LIPOPROTEIN; 1.
DR   Pfam; PF00127; Copper-bind; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   PRINTS; PR00695; CUNO2RDTASE.
DR   SUPFAM; SSF49503; Cupredoxins; 3.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
PE   4: Predicted;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR601287-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601287-1};
KW   Oxidoreductase {ECO:0000313|EMBL:CCM65846.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018291}.
FT   DOMAIN          123..215
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   DOMAIN          422..505
FT                   /note="Blue (type 1) copper"
FT                   /evidence="ECO:0000259|Pfam:PF00127"
FT   BINDING         152
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
FT   BINDING         157
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
FT   BINDING         192
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
FT   BINDING         193
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
FT   BINDING         201
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
FT   BINDING         206
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
FT   BINDING         350
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601287-1"
SQ   SEQUENCE   506 AA;  54013 MW;  117849E189B66BA7 CRC64;
     MESQTHLHKT KLQRRTMLGM LASTPVVVAA CTDNDLGADG SSAALAAEVV PEMVPLSAIQ
     EADPKEVHLS YAPAVPPTIT RKEPRRFDVH LEAVEGMAML DPANDVMTEK WGFKVAGDKT
     DVSGVPGPVI RGRVGDVVRI TLSNPTTGKH PHNIDFHSVT GMHGGASDLL VAPGESAAIQ
     ARLLYPGAFM YHCTAEDTLH HIAMGMYGMF IVDPAEPLPE VEHEWAVMQS EWYVDAPDAS
     GMAKFNRDRV TNEDPRYVTF NGSVGAIADD NSLKMKLGER SRIYFVNEGL NLTANFHPIG
     SHWDKVYPEA ATHPDNSIIR GSQSTSVVAG GGTVVEMLGM SPSSIVLVDH ALTRAFDKGA
     IGHVDIDGKE DPEIYSKIEP PKGGSGGGEV ITPTTAAAAV DPDTPVETTE VTIPKGSFDP
     ANAATAYSPP TIKVAVGDKV TWSNKDTVFH TVTSGKSDGS KATPDGKFNS GNIEAGDEFS
     FTFDTAGEYP YHCEPHPWMR GTVIVG
//
DBGET integrated database retrieval system