ANIA_NEIGO
ID ANIA_NEIGO Reviewed; 392 AA.
AC Q02219;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Copper-containing nitrite reductase;
DE EC=1.7.2.1;
DE AltName: Full=Major outer membrane protein Pan 1;
DE Flags: Precursor;
GN Name=aniA;
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=R10;
RX PubMed=1383156; DOI=10.1128/iai.60.11.4695-4703.1992;
RA Hoehn G.T., Clark V.L.;
RT "Isolation and nucleotide sequence of the gene (aniA) encoding the major
RT anaerobically induced outer membrane protein of Neisseria gonorrhoeae.";
RL Infect. Immun. 60:4695-4703(1992).
RN [2]
RP PALMITOYLATION AT CYS-19, AND DIACYLGLYCEROL AT CYS-19.
RC STRAIN=ATCC 33084 / F62 / M-1914;
RX PubMed=1398981; DOI=10.1128/iai.60.11.4704-4708.1992;
RA Hoehn G.T., Clark V.L.;
RT "The major anaerobically induced outer membrane protein of Neisseria
RT gonorrhoeae, Pan 1, is a lipoprotein.";
RL Infect. Immun. 60:4704-4708(1992).
RN [3]
RP FUNCTION, AND INDUCTION.
RC STRAIN=MS11;
RX PubMed=9413436; DOI=10.1007/s004380050597;
RA Mellies J., Jose J., Meyer T.F.;
RT "The Neisseria gonorrhoeae gene aniA encodes an inducible nitrite
RT reductase.";
RL Mol. Gen. Genet. 256:525-532(1997).
RN [4]
RP TRANSCRIPTIONAL REGULATION BY FNR AND NARP.
RC STRAIN=ATCC 33084 / F62 / M-1914;
RX PubMed=9882668; DOI=10.1128/jb.181.2.541-551.1999;
RA Householder T.C., Belli W.A., Lissenden S., Cole J.A., Clark V.L.;
RT "cis- and trans-acting elements involved in regulation of aniA, the gene
RT encoding the major anaerobically induced outer membrane protein in
RT Neisseria gonorrhoeae.";
RL J. Bacteriol. 181:541-551(1999).
RN [5]
RP PROTECTION AGAINST KILLING BY HUMAN SERA.
RC STRAIN=ATCC 33084 / F62 / M-1914;
RX PubMed=10858263; DOI=10.1128/iai.68.7.4368-4369.2000;
RA Cardinale J.A., Clark V.L.;
RT "Expression of AniA, the major anaerobically induced outer membrane protein
RT of Neisseria gonorrhoeae, provides protection against killing by normal
RT human sera.";
RL Infect. Immun. 68:4368-4369(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 42-364 IN COMPLEX WITH SUBSTRATE
RP AND COPPER IONS, AND SUBUNIT.
RX PubMed=11827480; DOI=10.1006/jmbi.2001.5251;
RA Boulanger M.J., Murphy M.E.P.;
RT "Crystal structure of the soluble domain of the major anaerobically induced
RT outer membrane protein (AniA) from pathogenic Neisseria: a new class of
RT copper-containing nitrite reductases.";
RL J. Mol. Biol. 315:1111-1127(2002).
CC -!- FUNCTION: Catalyzes the reduction of nitrite to nitric oxide (NO),
CC probably with azurin as electron donor. Essential for growth and
CC survival in oxygen-depleted environments. Can also provide protection
CC against killing by normal human sera. {ECO:0000269|PubMed:9413436}.
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 -!- COFACTOR:
CC Name=Cu(+); Xref=ChEBI:CHEBI:49552;
CC Note=Binds 1 Cu(+) ion.;
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Note=Binds 1 Cu(2+) ion.;
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:11827480}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- INDUCTION: By anaerobic and microaerophilic conditions in the presence
CC of nitrite. Regulated by the gonococcal fnr and NarP homologs.
CC {ECO:0000269|PubMed:1383156, ECO:0000269|PubMed:9413436,
CC ECO:0000269|PubMed:9882668}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:1398981}.
CC -!- MISCELLANEOUS: Undetected during aerobic growth.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; M97926; AAA25462.1; -; Genomic_DNA.
DR PIR; A49208; A49208.
DR RefSeq; WP_003700168.1; NZ_SAWD01000054.1.
DR PDB; 1KBV; X-ray; 1.95 A; A/B/C/D/E/F=42-364.
DR PDB; 1KBW; X-ray; 2.40 A; A/B/C/D/E/F=42-364.
DR PDBsum; 1KBV; -.
DR PDBsum; 1KBW; -.
DR AlphaFoldDB; Q02219; -.
DR SMR; Q02219; -.
DR PATRIC; fig|485.42.peg.2461; -.
DR EvolutionaryTrace; Q02219; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR001287; NO2-reductase_Cu.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR PRINTS; PR00695; CUNO2RDTASE.
DR SUPFAM; SSF49503; SSF49503; 2.
DR TIGRFAMs; TIGR02376; Cu_nitrite_red; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Copper; Lipoprotein; Membrane;
KW Metal-binding; Oxidoreductase; Palmitate; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT CHAIN 19..392
FT /note="Copper-containing nitrite reductase"
FT /id="PRO_0000002997"
FT DOMAIN 101..195
FT /note="Plastocyanin-like 1"
FT DOMAIN 245..346
FT /note="Plastocyanin-like 2"
FT REPEAT 368..372
FT /note="1"
FT REPEAT 373..377
FT /note="2"
FT REPEAT 378..382
FT /note="3"
FT REPEAT 383..387
FT /note="4"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..387
FT /note="4 X 5 AA tandem repeats of A-A-S-A-P"
FT BINDING 134
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 1 copper site"
FT BINDING 139
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 2 copper site"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11827480"
FT BINDING 174
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 2 copper site"
FT BINDING 175
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 1 copper site"
FT BINDING 183
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 1 copper site"
FT BINDING 188
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 1 copper site"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11827480"
FT BINDING 329
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 2 copper site"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:1398981"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:1398981"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 78..93
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:1KBV"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:1KBV"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:1KBV"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 204..214
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:1KBV"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:1KBV"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:1KBV"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 262..274
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:1KBV"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 310..318
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 322..330
FT /evidence="ECO:0007829|PDB:1KBV"
FT HELIX 332..336
FT /evidence="ECO:0007829|PDB:1KBV"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:1KBV"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:1KBV"
SQ SEQUENCE 392 AA; 40954 MW; A4707CC87B923C97 CRC64;
MKRQALAAMI ASLFALAACG GEQAAQAPAE TPAASAEAAS SAAQATAETP AGELPVIDAV
TTHAPEVPPA IDRDYPAKVR VKMETVEKTM KMDDGVEYRY WTFDGDVPGR MIRVREGDTV
EVEFSNNPSS TVPHNVDFHA ATGQGGGAAA TFTAPGRTST FSFKALQPGL YIYHCAVAPV
GMHIANGMYG LILVEPKEGL PKVDKEFYIV QGDFYTKGKK GAQGLQPFDM DKAVAEQPEY
VVFNGHVGSI AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN
VQSTIVPAGG SAIVEFKVDI PGSYTLVDHS IFRAFNKGAL GQLKVEGAEN PEIMTQKLSD
TAYAGSGAAS APAASAPAAS APAASASEKS VY
