ID B1P8C4_MORCA Unreviewed; 518 AA.
AC B1P8C4;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Copper-containing nitrite reductase {ECO:0000256|ARBA:ARBA00017290, ECO:0000256|RuleBase:RU365025};
DE EC=1.7.2.1 {ECO:0000256|ARBA:ARBA00011882, ECO:0000256|RuleBase:RU365025};
DE Flags: Fragment;
GN Name=msp78 {ECO:0000313|EMBL:ACA52191.1};
GN Synonyms=aniA {ECO:0000313|EMBL:ACJ68080.1};
OS Moraxella catarrhalis (Branhamella catarrhalis).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=480 {ECO:0000313|EMBL:ACA52191.1};
RN [1] {ECO:0000313|EMBL:ACA52191.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 43617 {ECO:0000313|EMBL:ACA52191.1};
RX PubMed=18227159; DOI=10.1128/IAI.01253-07;
RA Ruckdeschel E.A., Kirkham C., Lesse A.J., Hu Z., Murphy T.F.;
RT "Mining the Moraxella catarrhalis genome: identification of potential
RT vaccine antigens expressed during human infection.";
RL Infect. Immun. 76:1599-1607(2008).
RN [2] {ECO:0000313|EMBL:ACJ68080.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=7169 {ECO:0000313|EMBL:ACJ68085.1}, ETSU-9
RC {ECO:0000313|EMBL:ACJ68089.1}, and O35E {ECO:0000313|EMBL:ACJ68080.1};
RX PubMed=18820017; DOI=10.1128/JB.01032-08;
RA Wang W., Richardson A.R., Martens-Habbena W., Stahl D.A., Fang F.C.,
RA Hansen E.J.;
RT "Identification of a repressor of a truncated denitrification pathway in
RT Moraxella catarrhalis.";
RL J. Bacteriol. 190:7762-7772(2008).
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 ECO:0000256|RuleBase:RU365025};
CC -!- COFACTOR:
CC Name=Cu(+); Xref=ChEBI:CHEBI:49552;
CC Evidence={ECO:0000256|RuleBase:RU365025};
CC Note=Binds 1 Cu(+) ion. {ECO:0000256|RuleBase:RU365025};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|RuleBase:RU365025};
CC Note=Binds 1 Cu(+) ion. {ECO:0000256|RuleBase:RU365025};
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233,
CC ECO:0000256|RuleBase:RU365025}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|RuleBase:RU365025}.
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DR EMBL; EU339313; ACA52191.1; -; Genomic_DNA.
DR EMBL; EU861986; ACJ68080.1; -; Genomic_DNA.
DR EMBL; EU861987; ACJ68085.1; -; Genomic_DNA.
DR EMBL; EU861988; ACJ68089.1; -; Genomic_DNA.
DR AlphaFoldDB; B1P8C4; -.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme 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; 2.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR001287; NO2-reductase_Cu.
DR NCBIfam; TIGR02376; Cu_nitrite_red; 1.
DR PANTHER; PTHR35008:SF8; BLL4482 PROTEIN; 1.
DR PANTHER; PTHR35008; BLL4482 PROTEIN-RELATED; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00695; CUNO2RDTASE.
DR SUPFAM; SSF49503; Cupredoxins; 2.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|PIRSR:PIRSR601287-1, ECO:0000256|RuleBase:RU365025};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601287-1};
KW Oxidoreductase {ECO:0000256|RuleBase:RU365025}.
FT DOMAIN 409..497
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 155
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 160
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 195
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 196
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 204
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 209
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"
FT NON_TER 518
FT /evidence="ECO:0000313|EMBL:ACA52191.1"
SQ SEQUENCE 518 AA; 55247 MW; 00CE1B7E19F0E621 CRC64;
MALKKITGNL SIRRTHMSKP TLIKTTLICA LSALMLSGCS NQADKAAQPK SSTVDAAAKT
ANADNAASQE HQGELPVIDA IVTHAPEVPP PVDRDHPAKV VVKMETVEKV MRLADGVEYQ
FWTFGGQVPG QMIRVREGDT IEVQFSNHPD SKMPHNVDFH AATGPGGGAE ASFTAPGHTS
TFSFKALQPG LYVYHCAVAP VGMHIANGMY GLILVEPKEG LPKVDKEYYV MQGDFYTKGK
YGEQGLQPFD MEKAIREDAE YVVFNGSVGA LTGENALKAK VGETVRLFVG NGGPNLTSSF
HVIGEIFDKV HFEGGKGENH NIQTTLIPAG GAAITEFKVD VPGDYVLVDH AIFRAFNKGA
LGILKVEGEE NHEIYSHKQT DAVYLPEGAP QAIDTQEAPK TPAPANLQEQ IKAGKATYDS
NCAACHQPDG KGVPNAFPPL ANSDYLNADH ARAASIVANG LSGKITVNGN QYESVMPAIA
LSDQQIANVI TYTLNSFGNK GGQLSADDVA KAKKTKPN
//
