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Database: UniProt
Entry: Q2W7H6_MAGSA
LinkDB: Q2W7H6_MAGSA
Original site: Q2W7H6_MAGSA 
ID   Q2W7H6_MAGSA            Unreviewed;       540 AA.
AC   Q2W7H6;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=Nitrite reductase {ECO:0000313|EMBL:BAE50199.1};
GN   OrderedLocusNames=amb1395 {ECO:0000313|EMBL:BAE50199.1};
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE50199.1, ECO:0000313|Proteomes:UP000007058};
RN   [1] {ECO:0000313|EMBL:BAE50199.1, ECO:0000313|Proteomes:UP000007058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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DR   EMBL; AP007255; BAE50199.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2W7H6; -.
DR   STRING; 342108.amb1395; -.
DR   KEGG; mag:amb1395; -.
DR   HOGENOM; CLU_025262_0_0_5; -.
DR   OrthoDB; 5290932at2; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.140.10.20; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR003143; Cyt_cd1_C_sf.
DR   InterPro; IPR011048; Haem_d1_sf.
DR   Pfam; PF02239; Cytochrom_D1; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   SUPFAM; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   4: Predicted;
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, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Reference proteome {ECO:0000313|Proteomes:UP000007058};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..540
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004218240"
FT   DOMAIN          32..109
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   540 AA;  59529 MW;  2CAAD225425E6767 CRC64;
     MWKGVRNALL LTALPFAMSG AAFAQEATLS KEAKEASAKI YFERCAGCHG VLRKGATGKN
     LEPANTTKLG QARLEKILTN GTDGGMVNFD DILTKDEIKN MATYIQMTPD VPPEWGIKEM
     TASWKVTVKP EDRPKKQMNK VNLKNVFSVT LRDTGEIALI DGDTKKIWTI IKTGYAVHIS
     RLSASGRFVY VIGRDGKLDM IDLWMETPAV VATIKIGMDA RSVETSKFKG FEDKYAVAGS
     YWPPQYVIMD GADLKPLKIV STRGITVDGE YHPEPRVASI VASMIKPEWV INIKETGLIK
     LVDYSDIKNL KETTIESAKF LHDGGWDASK RYFLVAANAS NKVAVVDTKD GKLAGLVDTK
     SKPHPGRGAN FNHPKFGPVW ATSHLGADVI TLIGTDPAKH KDQAWKVVAE LKNHGAGSLF
     VKTHPKSNNL WADAPLFPEK DMAESVTVYD IKNLDKGPEV INIAKLADLP ETKAVKRAVQ
     AEYNEKGDEV WFSIWAGKTD PSAIVVMDDK TRKVKAVIKD PKLITPTGKF NVYNTQHDIY
//
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