ID NRFA_ECOLI STANDARD; PRT; 478 AA. AC P0ABK9; P32050; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 07-FEB-2006 (Rel. 49, Last annotation update) DE Cytochrome c-552 precursor (EC 1.7.2.2) (Ammonia-forming cytochrome c DE nitrite reductase) (Cytochrome c nitrite reductase). GN Name=nrfA; OrderedLocusNames=b4070; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 27-42 AND RP 150-167. RC STRAIN=K12; RX MEDLINE=95020657; PubMed=7934939; 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 [GENOMIC DNA]. RC STRAIN=K12 / MG1655; RX MEDLINE=94089392; PubMed=8265357; 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; RX MEDLINE=97426617; 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 CHARACTERIZATION AS A CYTOCHROME C. RX MEDLINE=94314186; 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 [5] RP HEME-BINDING, MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-126. RX MEDLINE=98254140; PubMed=9593308; 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 [6] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), MAGNETIC CIRCULAR DICHROISM, RP AND EPR SPECTROSCOPY. RX MEDLINE=21852612; 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: Terminal reductase of the formate-dependent pathway for CC nitrite reduction to ammonia. CC -!- SUBCELLULAR LOCATION: Periplasmic. CC -!- INDUCTION: Full induction attained in the presence of nitrite. CC Subject to glucose and nitrate repression. CC -!- MASS SPECTROMETRY: MW=53590; METHOD=MALDI; RANGE=27-478; CC NOTE=Ref.5. 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; -; Unassigned_DNA. DR EMBL; U00096; AAC77040.1; -; Genomic_DNA. DR PIR; S39590; S39590. DR PDB; 1GU6; X-ray; A/C/E/G=27-478. DR EchoBASE; EB1729; -. DR EcoGene; EG11781; nrfA. DR InterPro; IPR003321; Cyt_c552. DR InterPro; IPR011031; Multihaem_cyt. DR Pfam; PF02335; Cytochrom_C552; 1. DR PROSITE; PS51008; MULTIHEME_CYTC; 1. KW 3D-structure; Calcium; Complete proteome; Direct protein sequencing; KW Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; KW Periplasmic; 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 STRAND 67 67 FT HELIX 68 71 FT TURN 73 73 FT HELIX 74 78 FT TURN 79 81 FT HELIX 83 85 FT TURN 86 86 FT STRAND 89 89 FT HELIX 94 96 FT HELIX 97 103 FT HELIX 105 107 FT TURN 113 114 FT STRAND 119 119 FT HELIX 120 123 FT TURN 124 126 FT TURN 128 128 FT HELIX 129 143 FT STRAND 146 146 FT HELIX 147 150 FT TURN 151 153 FT HELIX 160 163 FT STRAND 164 164 FT TURN 166 167 FT HELIX 169 172 FT TURN 173 174 FT STRAND 178 178 FT HELIX 183 191 FT TURN 192 193 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 TURN 230 231 FT HELIX 235 244 FT TURN 245 246 FT STRAND 250 251 FT TURN 253 255 FT STRAND 258 259 FT HELIX 266 272 FT HELIX 274 277 FT TURN 278 279 FT HELIX 282 286 FT STRAND 289 291 FT TURN 293 294 FT STRAND 297 299 FT HELIX 306 312 FT TURN 313 313 FT HELIX 314 316 FT TURN 317 317 FT HELIX 322 359 FT TURN 360 361 FT HELIX 364 385 FT TURN 388 389 FT HELIX 390 393 FT HELIX 395 421 FT TURN 422 424 FT HELIX 437 443 FT TURN 444 445 FT HELIX 448 472 FT TURN 473 474 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 //