ID NRFA_ECOLI Reviewed; 478 AA. AC P0ABK9; P32050; Q2M6N4; DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 01-MAY-2013, entry version 74. DE RecName: Full=Cytochrome c-552; DE EC=1.7.2.2; DE AltName: Full=Ammonia-forming cytochrome c nitrite reductase; DE Short=Cytochrome c nitrite reductase; DE Flags: Precursor; GN Name=nrfA; OrderedLocusNames=b4070, JW4031; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 27-42 AND RP 150-167. RC STRAIN=K12; RX PubMed=7934939; DOI=10.1111/j.1365-2958.1993.tb01255.x; RA Darwin A., Hussain H.A., Griffiths L., Grove J., Sambongi Y., RA Busby S., Cole J.; RT "Regulation and sequence of the structural gene for cytochrome c552 RT from Escherichia coli: not a hexahaem but a 50 kDa tetrahaem nitrite RT reductase."; RL Mol. Microbiol. 9:1255-1265(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=8265357; DOI=10.1093/nar/21.23.5408; RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., RA Daniels D.L.; RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the RT region from 89.2 to 92.8 minutes."; RL Nucleic Acids Res. 21:5408-5417(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP CHARACTERIZATION AS A CYTOCHROME C. RX PubMed=8039676; DOI=10.1016/0378-1097(94)90397-2; RA Iobbi-Nivol C., Crooke H., Griffiths L., Grov J., Hussain H., RA Pommier J., Mejean V., Cole J.A.; RT "A reassessment of the range of c-type cytochromes synthesized by RT Escherichia coli K-12."; RL FEMS Microbiol. Lett. 119:89-94(1994). RN [6] RP HEME-BINDING, MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-126. RX PubMed=9593308; DOI=10.1046/j.1365-2958.1998.00792.x; RA Eaves D.J., Grove J., Staudenmann W., James P., Poole R.K., RA White S.A., Griffiths I., Cole J.A.; RT "Involvement of products of the nrfEFG genes in the covalent RT attachment of haem c to a novel cysteine-lysine motif in the RT cytochrome c552 nitrite reductase from Escherichia coli."; RL Mol. Microbiol. 28:205-216(1998). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), MAGNETIC CIRCULAR DICHROISM, RP AND EPR SPECTROSCOPY. RX PubMed=11863430; DOI=10.1021/bi015765d; RA Bamford V.A., Angove H.C., Seward H.E., Thomson A.J., Cole J.A., RA Butt J.N., Hemmings A.M., Richardson D.J.; RT "Structure and spectroscopy of the periplasmic cytochrome c nitrite RT reductase from Escherichia coli."; RL Biochemistry 41:2921-2931(2002). CC -!- FUNCTION: Plays a role in nitrite reduction. CC -!- CATALYTIC ACTIVITY: NH(3) + 2 H(2)O + 6 ferricytochrome c = CC nitrite + 6 ferrocytochrome c + 7 H(+). CC -!- COFACTOR: Binds 1 calcium ion per monomer. CC -!- COFACTOR: Binds 5 heme groups covalently per monomer. CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation). CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- INDUCTION: Full induction attained in the presence of nitrite. CC Subject to glucose and nitrate repression. CC -!- MASS SPECTROMETRY: Mass=53590; Method=MALDI; Range=27-478; CC Source=PubMed:9593308; CC -!- SIMILARITY: Belongs to the cytochrome c-552 family. 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; X72298; CAA51048.1; -; Genomic_DNA. DR EMBL; U00006; AAC43164.1; -; Genomic_DNA. DR EMBL; U00096; AAC77040.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78072.1; -; Genomic_DNA. DR PIR; S39590; S39590. DR RefSeq; NP_418494.1; NC_000913.2. DR RefSeq; YP_492213.1; NC_007779.1. DR PDB; 1GU6; X-ray; 2.50 A; A/C/E/G=27-478. DR PDB; 2RDZ; X-ray; 1.74 A; A/B/C/D=27-478. DR PDB; 2RF7; X-ray; 2.04 A; A/B/C/D=37-477. DR PDB; 3L1T; X-ray; 2.30 A; A/B/C/D=27-478. DR PDB; 3TOR; X-ray; 2.00 A; A/B/C/D=27-478. DR PDBsum; 1GU6; -. DR PDBsum; 2RDZ; -. DR PDBsum; 2RF7; -. DR PDBsum; 3L1T; -. DR PDBsum; 3TOR; -. DR ProteinModelPortal; P0ABK9; -. DR SMR; P0ABK9; 37-477. DR DIP; DIP-36021N; -. DR IntAct; P0ABK9; 3. DR STRING; 511145.b4070; -. DR PaxDb; P0ABK9; -. DR PRIDE; P0ABK9; -. DR EnsemblBacteria; AAC77040; AAC77040; b4070. DR EnsemblBacteria; BAE78072; BAE78072; BAE78072. DR GeneID; 12930411; -. DR GeneID; 948571; -. DR KEGG; ecj:Y75_p3957; -. DR KEGG; eco:b4070; -. DR PATRIC; 32123689; VBIEscCol129921_4193. DR EchoBASE; EB1729; -. DR EcoGene; EG11781; nrfA. DR eggNOG; COG3303; -. DR HOGENOM; HOG000278511; -. DR KO; K03385; -. DR OMA; QVTFPWD; -. DR ProtClustDB; PRK11125; -. DR BioCyc; EcoCyc:CYTOCHROMEC552-MONOMER; -. DR BioCyc; ECOL316407:JW4031-MONOMER; -. DR BioCyc; MetaCyc:CYTOCHROMEC552-MONOMER; -. DR UniPathway; UPA00653; -. DR EvolutionaryTrace; P0ABK9; -. DR Genevestigator; P0ABK9; -. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc. DR GO; GO:0005509; F:calcium ion binding; IEA:HAMAP. DR GO; GO:0020037; F:heme binding; IDA:EcoCyc. DR GO; GO:0005506; F:iron ion binding; IEA:HAMAP. DR GO; GO:0042279; F:nitrite reductase (cytochrome, ammonia-forming) activity; IDA:EcoCyc. DR GO; GO:0019645; P:anaerobic electron transport chain; IMP:EcoCyc. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.710.10; -; 1. DR HAMAP; MF_01182; Cytochrom_C552; 1; -. DR InterPro; IPR023155; Cyt_c-552/4. DR InterPro; IPR003321; Cyt_c552. DR InterPro; IPR017570; Cyt_c_NO2Rdtase_formate-dep. DR InterPro; IPR011031; Multihaem_cyt. DR Pfam; PF02335; Cytochrom_C552; 1. DR PIRSF; PIRSF000243; Cyt_c552; 1. DR TIGRFAMs; TIGR03152; cyto_c552_HCOOH; 1. DR PROSITE; PS51008; MULTIHEME_CYTC; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Complete proteome; Direct protein sequencing; KW Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; KW Periplasm; Reference proteome; Signal; Transport. FT SIGNAL 1 26 FT CHAIN 27 478 Cytochrome c-552. FT /FTId=PRO_0000006578. FT METAL 94 94 Iron (heme 3 axial ligand). FT METAL 126 126 Iron (heme 1 axial ligand). FT METAL 164 164 Iron (heme 2 axial ligand). FT METAL 213 213 Iron (heme 3 axial ligand). FT METAL 215 215 Calcium. FT METAL 216 216 Calcium; via carbonyl oxygen. FT METAL 261 261 Calcium; via carbonyl oxygen. FT METAL 263 263 Calcium. FT METAL 275 275 Iron (heme 5 axial ligand). FT METAL 286 286 Iron (heme 4 axial ligand). FT METAL 301 301 Iron (heme 2 axial ligand). FT METAL 318 318 Iron (heme 5 axial ligand). FT METAL 393 393 Iron (heme 4 axial ligand). FT BINDING 122 122 Heme 1 (covalent). FT BINDING 125 125 Heme 1 (covalent). FT BINDING 160 160 Heme 2 (covalent). FT BINDING 163 163 Heme 2 (covalent). FT BINDING 209 209 Heme 3 (covalent). FT BINDING 212 212 Heme 3 (covalent). FT BINDING 216 216 Substrate (By similarity). FT BINDING 264 264 Substrate (By similarity). FT BINDING 282 282 Heme 4 (covalent). FT BINDING 285 285 Heme 4 (covalent). FT BINDING 314 314 Heme 5 (covalent). FT BINDING 317 317 Heme 5 (covalent). FT MUTAGEN 126 126 K->H,I,L: Almost complete loss of nitrite FT reductase activity. FT HELIX 42 45 FT TURN 46 48 FT HELIX 50 57 FT HELIX 58 61 FT HELIX 68 71 FT HELIX 74 78 FT TURN 79 81 FT HELIX 83 85 FT HELIX 94 96 FT HELIX 97 103 FT HELIX 105 107 FT STRAND 116 119 FT HELIX 120 123 FT TURN 124 126 FT HELIX 129 137 FT HELIX 139 143 FT STRAND 144 146 FT HELIX 147 150 FT TURN 151 153 FT HELIX 160 163 FT HELIX 169 172 FT HELIX 183 191 FT HELIX 196 198 FT HELIX 201 209 FT TURN 210 212 FT STRAND 217 219 FT TURN 220 223 FT STRAND 224 226 FT HELIX 235 244 FT STRAND 249 251 FT TURN 253 255 FT HELIX 266 272 FT HELIX 274 277 FT HELIX 282 286 FT STRAND 289 291 FT STRAND 297 299 FT HELIX 306 312 FT HELIX 314 316 FT HELIX 322 359 FT HELIX 364 385 FT HELIX 390 393 FT HELIX 395 422 FT HELIX 437 443 FT HELIX 448 472 SQ SEQUENCE 478 AA; 53703 MW; F965E986412A0456 CRC64; MTRIKINARR IFSLLIPFFF FTSVHAEQTA APAKPVTVEA KNETFAPQHP DQYLSWKATS EQSERVDALA EDPRLVILWA GYPFSRDYNK PRGHAFAVTD VRETLRTGAP KNAEDGPLPM ACWSCKSPDV ARLIQKDGED GYFHGKWARG GPEIVNNLGC ADCHNTASPE FAKGKPELTL SRPYAARAME AIGKPFEKAG RFDQQSMVCG QCHVEYYFDG KNKAVKFPWD DGMKVENMEQ YYDKIAFSDW TNSLSKTPML KAQHPEYETW TAGIHGKNNV TCIDCHMPKV QNAEGKLYTD HKIGNPFDNF AQTCANCHTQ DKAALQKVVA ERKQSINDLK IKVEDQLVHA HFEAKAALDA GATEAEMKPI QDDIRHAQWR WDLAIASHGI HMHAPEEGLR MLGTAMDKAA DARTKLARLL ATKGITHEIQ IPDISTKEKA QQAIGLNMEQ IKAEKQDFIK TVIPQWEEQA RKNGLLSQ //