NRFA_SULDE
ID NRFA_SULDE Reviewed; 514 AA.
AC Q9Z4P4;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cytochrome c-552;
DE EC=1.7.2.2 {ECO:0000269|PubMed:7999130};
DE AltName: Full=Ammonia-forming cytochrome c nitrite reductase {ECO:0000303|PubMed:7999130};
DE Short=Cytochrome c nitrite reductase {ECO:0000303|PubMed:10440380, ECO:0000303|PubMed:7999130};
DE Flags: Precursor;
GN Name=nrfA;
OS Sulfurospirillum deleyianum.
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Sulfurospirillaceae; Sulfurospirillum.
OX NCBI_TaxID=65553;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN
RP COMPLEX WITH CALCIUM; HEME AND SULFATE, COFACTOR, AND SUBUNIT.
RX PubMed=10440380; DOI=10.1038/22802;
RA Einsle O., Messerschmidt A., Stach P., Bourenkov G.P., Bartunik H.D.,
RA Huber R., Kroneck P.M.H.;
RT "Structure of cytochrome c nitrite reductase.";
RL Nature 400:476-480(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, HEME-BINDING, AND COFACTOR.
RX PubMed=7999130; DOI=10.1006/bbrc.1994.2751;
RA Schumacher W., Hole U., Kroneck P.M.H.;
RT "Ammonia-forming cytochrome c nitrite reductase from Sulfurospirillum
RT deleyianum is a tetraheme protein: new aspects of the molecular composition
RT and spectroscopic properties.";
RL Biochem. Biophys. Res. Commun. 205:911-916(1994).
CC -!- FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming six
CC electrons in the process (PubMed:7999130). Has very low activity toward
CC hydroxylamine, and even lower activity toward sulfite. Sulfite
CC reductase activity is maximal at neutral pH (By similarity).
CC {ECO:0000250|UniProtKB:L0DSL2, ECO:0000269|PubMed:7999130}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6 Fe(III)-[cytochrome c] + 2 H2O + NH4(+) = 6 Fe(II)-
CC [cytochrome c] + 8 H(+) + nitrite; Xref=Rhea:RHEA:13089, Rhea:RHEA-
CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.2;
CC Evidence={ECO:0000269|PubMed:7999130};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000269|PubMed:10440380};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:10440380, ECO:0000269|PubMed:7999130};
CC Note=Binds 5 heme c groups covalently per monomer.
CC {ECO:0000269|PubMed:10440380};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC {ECO:0000305|PubMed:7999130}.
CC -!- SUBUNIT: Homodimer (PubMed:7999130). Probably also exists as a
CC membrane-associated heterooligomeric complex (PubMed:10440380).
CC {ECO:0000269|PubMed:10440380, ECO:0000269|PubMed:7999130}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:7999130}.
CC -!- MISCELLANEOUS: X-ray crystallographic analysis includes a sulfate ion
CC that is thought to be at the substrate-binding site.
CC {ECO:0000269|PubMed:10440380}.
CC -!- SIMILARITY: Belongs to the cytochrome c-552 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB37320.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AJ133037; CAB37320.2; ALT_INIT; mRNA.
DR PDB; 1QDB; X-ray; 1.90 A; A/B/C=42-514.
DR PDBsum; 1QDB; -.
DR AlphaFoldDB; Q9Z4P4; -.
DR SMR; Q9Z4P4; -.
DR OMA; MHAPDVM; -.
DR UniPathway; UPA00653; -.
DR EvolutionaryTrace; Q9Z4P4; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042279; F:nitrite reductase (cytochrome, ammonia-forming) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR CDD; cd00548; NrfA-like; 1.
DR HAMAP; MF_01182; Cytochrom_C552; 1.
DR InterPro; IPR003321; Cyt_c552.
DR InterPro; IPR017570; Cyt_c_NO2Rdtase_formate-dep.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR PANTHER; PTHR30633; PTHR30633; 1.
DR Pfam; PF02335; Cytochrom_C552; 1.
DR PIRSF; PIRSF000243; Cyt_c552; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Electron transport; Heme; Iron; Metal-binding;
KW Oxidoreductase; Periplasm; Signal; Transport.
FT SIGNAL 1..21
FT CHAIN 22..514
FT /note="Cytochrome c-552"
FT /id="PRO_0000006583"
FT BINDING 101
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 129
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 132
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 133
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 167
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 170
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 171
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 210
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 213
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 214
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 217
FT /ligand="substrate"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 282
FT /ligand="substrate"
FT BINDING 293
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 300
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 303
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 304
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 318
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 332
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 335
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 336
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:1QDB"
FT BINDING 411
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:1QDB"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:1QDB"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1QDB"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:1QDB"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:1QDB"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:1QDB"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1QDB"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:1QDB"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:1QDB"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:1QDB"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 253..262
FT /evidence="ECO:0007829|PDB:1QDB"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1QDB"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 284..290
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:1QDB"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:1QDB"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:1QDB"
FT TURN 332..335
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 340..377
FT /evidence="ECO:0007829|PDB:1QDB"
FT TURN 382..385
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 386..404
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 413..440
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 454..461
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 465..477
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 479..489
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:1QDB"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:1QDB"
SQ SEQUENCE 514 AA; 57611 MW; E63C119D4FA98562 CRC64;
MKFKLLLAGS LVAVGAMALL ASNINEKEKQ RVELAKAPSE AGIAGKEKSE EWAKYYPRQF
DSWKKTKEYD SFTDMLAKDP ALVIAWSGYA FSKDYNSPRG HYYALQDNVN SLRTGAPVDA
KTGPLPTACW TCKSPDVPRL IEEDGELEYF TGKWAKYGSQ IVNVIGCANC HDDKTAELKV
RVPHLNRGLQ AAGLKTFEES THQDKRTLVC AQCHVEYYFK KTEWKDAKGA DKTAMVVTLP
WANGVGKDGN AGVEGMIKYY DEINFSDWTH NISKTPMLKA QHPGFEFWKS GIHGQKGVSC
ADCHMPYTQE GSVKYSDHQV KENPLDSMDQ SCMNCHRESE SKLRGIVHQK YERKEFLNKV
AFDNIGKAHL ETGKAIEAGA SDEELKEVRK LIRHGQFKAD MAIAAHGNYF HAPEETLRLL
AAGSDDAQKA RLLLVKILAK HGVMDYIAPD FDTKDKAQKL AKVDIAALAA EKMKFKQTLE
QEWKKEAKAK GRANPELYKD VDTINDGKSS WNKK
