ID A0A366ZJ34_9ACTN Unreviewed; 865 AA.
AC A0A366ZJ34;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Copper-containing nitrite reductase {ECO:0000256|ARBA:ARBA00017290};
DE EC=1.7.2.1 {ECO:0000256|ARBA:ARBA00011882};
GN ORFNames=DQ238_15925 {ECO:0000313|EMBL:RBY77200.1};
OS Geodermatophilus sp. TF02-6.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=2250575 {ECO:0000313|EMBL:RBY77200.1, ECO:0000313|Proteomes:UP000253027};
RN [1] {ECO:0000313|EMBL:RBY77200.1, ECO:0000313|Proteomes:UP000253027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF02-6 {ECO:0000313|EMBL:RBY77200.1,
RC ECO:0000313|Proteomes:UP000253027};
RA Ennis N., Dharumadurai D., Sevigny J., Hall J., Simposon S., Morris K.,
RA Thomas W.K., Tisa L.S.;
RT "Genome Sequence of Geodermatophilus sp. TF02-6.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-
CC [cytochrome c] + 2 H(+) + nitrite; Xref=Rhea:RHEA:15233, Rhea:RHEA-
CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00029301};
CC -!- COFACTOR:
CC Name=Cu(+); Xref=ChEBI:CHEBI:49552;
CC Evidence={ECO:0000256|ARBA:ARBA00001960,
CC ECO:0000256|PIRSR:PIRSR601287-1};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973,
CC ECO:0000256|PIRSR:PIRSR601287-1};
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}.
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:RBY77200.1}.
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DR EMBL; QOHF01000017; RBY77200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366ZJ34; -.
DR OrthoDB; 345021at2; -.
DR Proteomes; UP000253027; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; 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; cd11020; CuRO_1_CuNIR; 1.
DR CDD; cd04208; CuRO_2_CuNIR; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR028096; EfeO_Cupredoxin.
DR InterPro; IPR001287; NO2-reductase_Cu.
DR PANTHER; PTHR11709:SF218; FI03373P-RELATED; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR Pfam; PF13473; Cupredoxin_1; 1.
DR PRINTS; PR00695; CUNO2RDTASE.
DR SUPFAM; SSF49503; Cupredoxins; 3.
PE 4: Predicted;
KW Copper {ECO:0000256|PIRSR:PIRSR601287-1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601287-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253027};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 461..524
FT /note="EfeO-type cupredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF13473"
FT DOMAIN 611..718
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT REGION 393..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 656
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 661
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 695
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 696
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 704
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 709
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 846
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 865 AA; 87999 MW; 48D36949B3FC4705 CRC64;
MRDLPVVGWL TATAGVALVH PVVPAPRWLM IHLLLLGAVG HAILVWSRHF TEALLHTAPG
PGDRRTQSRR LLQFNAGAVL VVTGVVSATW PVTVAGAAAV AGAVGWHGAA LGRQLHRAPP
GRFRSTVRHH VVAAALLPVG ATLGTLLARG LGGPWQERAL LAHVVVNVLG WVGLTVVGTL
VTLWPAMLRT RIAEDAERAA RRALPVLAGA VVVAAGGALA GSRTLAVAGL AGYVAGLVLV
GRVLVATART RPPSSYPTWS VAAAVLWLTG CVAAATVAVG TAGSWAEAGD RLAWLTPFLA
AGFGAQVLLG ALSHLVPVAL GGGAVPVRAA NTVLDRGGPL RIAVVNAGLL VCVLPVPSVV
RVGASALVLA GLGAFVPLLF LAIGASRRAR AGDAGPGGGA VGGPHPPTTA ARPRGQAAGL
AVAGLAAVAL VVAAGVAVDP SALPDARALA AVPAADVVPT GRTTTVRVEA RDMRFTPETV
DVPAGDRLVV ELVNADDAAV HDLVLDSGAD SGRLAPGEST RLDVGVVGTD LEGWCSVVGH
RQMGMVLHVR AVGGTSSPAA GSAVDAAAGP GSAADDLDFA AEPGDGFTAH DPVLPPLTDE
RVHRLTLPVS EVEREVAPGV TQQLWTFGGS APGPVLHGRV GDVFEVTLVN DGTIGHSIDF
HAGALAPDGP MRTIPPGESL VYRFTATRAG VWMYHCSTAP MSAHIANGMF GAVVIEPDGL
PAVDRSYVLV QSELYLGPQG GPVDVAKLAE ERPDAVVFNG YADQYDARPL TAEVGERVRI
WVLDAGPNRA TSFHVVGGQF DTVYAEGTHL LQPGAGGSQV LALGPAQGGF VELTFPEAGR
YPVVSHVVVD AERGAHGVVE VSAGR
//
