(data stored in ACNUC7421 zone)

SWISSPROT: B2UI62_RALPJ

ID   B2UI62_RALPJ            Unreviewed;       851 AA.
AC   B2UI62;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   SubName: Full=Nitrite reductase (NAD(P)H), large subunit {ECO:0000313|EMBL:ACD29263.1};
GN   OrderedLocusNames=Rpic_4164 {ECO:0000313|EMBL:ACD29263.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29263.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S
CC       domain family. {ECO:0000256|SAAS:SAAS00570916}.
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DR   EMBL; CP001069; ACD29263.1; -; Genomic_DNA.
DR   STRING; 402626.Rpic_4164; -.
DR   EnsemblBacteria; ACD29263; ACD29263; Rpic_4164.
DR   KEGG; rpi:Rpic_4164; -.
DR   eggNOG; ENOG4107QZF; Bacteria.
DR   eggNOG; COG1251; LUCA.
DR   HOGENOM; HOG000196164; -.
DR   KO; K00362; -.
DR   OMA; PLVTQIM; -.
DR   BioCyc; RPIC402626:GH94-4159-MONOMER; -.
DR   Proteomes; UP000002566; Chromosome 2.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:InterPro.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:InterPro.
DR   Gene3D; 1.10.10.1100; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR012744; Nitri_red_NirB.
DR   InterPro; IPR017121; Nitrite_Rdtase_lsu.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   InterPro; IPR041575; Rubredoxin_C.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF18267; Rubredoxin_C; 1.
DR   PIRSF; PIRSF037149; NirB; 1.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55124; SSF55124; 1.
DR   TIGRFAMs; TIGR02374; nitri_red_nirB; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2UI62.
DR   SWISS-2DPAGE; B2UI62.
KW   4Fe-4S {ECO:0000256|SAAS:SAAS00296119};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   Heme {ECO:0000256|SAAS:SAAS00460474};
KW   Iron {ECO:0000256|SAAS:SAAS00296139};
KW   Iron-sulfur {ECO:0000256|SAAS:SAAS00296144};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00296121};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS00460503};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566}.
FT   DOMAIN        4    283       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      319    389       Rubredoxin_C. {ECO:0000259|Pfam:PF18267}.
FT   DOMAIN      423    470       Fer2_BFD. {ECO:0000259|Pfam:PF04324}.
FT   DOMAIN      559    621       NIR_SIR_ferr. {ECO:0000259|Pfam:PF03460}.
FT   DOMAIN      631    752       NIR_SIR. {ECO:0000259|Pfam:PF01077}.
SQ   SEQUENCE   851 AA;  92404 MW;  A7D4502EB4E0D02E CRC64;
     MTMKIVVIGH GMVGHKFLES LLHAPGHHLQ VTVLCEEPRP AYDRVHLSEF FTGKTAEELS
     LVAPGFFDRD DVVLKLNARA TAIDITAKTV TASTGEVLPY DKLVLASGSS PFVPPVPGRD
     RKDCFVYRTI EDLEAMAECG QRAKTGVVIG GGLLGLECAK ALRDMNLQTH VVEFAGRLMA
     MQVDDGGGRM LRRKIEDLGV TVHTQKNTSE IVDGETATHR LNFADGTHLE ADMVVFSAGI
     RPRDELARAC GLEVGERGGI VIDSECRTSA PDVYAIGECA LWGGKIYGLV APGYEMARIT
     AKQILAADDA SEFSGADMST KLKLMGVDVA SLGDAQGVTP GSRSVQFTDE RKQIYKKLVV
     SEDGKYLLGG VLVGDAAEYG TLLQMMLNRI ELPEAPEFLI LPQADGNARP ALGVDALPDS
     AQICSCNDVS KGALCQAVCA GATTVGALKD ATKAGTSCGG CVPLMTQVMK AEMKKQGLAV
     NNHICEHFPY SRQELYHLVR VGRIQSFEAL LEAHGSGMGC DICKPAVASI LASCWNDFVL
     KKEHASLQDS NDYFLANIQK DGTYSVVPRM PGGEVTADGL IAVGQVAKKY DLYTKITGGQ
     RVDLFGARLE QLPLIWEELI AAGFESGHAY GKSLRTVKSC VGSTWCRYGV GDSVGFAIAL
     ENRYKGLRSP HKIKFGVSGC TRECAEAQGK DVGIIATEKG WNLYVCGNGG MKPRHAELLA
     ADLDQETLIK YVDRFLMFYV RTADRLQRTS TWRDNLEGGL DYLKDVVIND KLGIVAELEA
     EMQHVVDTYQ DEWKTAVTNP DVRKRFRHFV NSEAKDANVV FVEERGQIRP ATVEERAKTR
     PVRIPVVAEA A
//

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