ID   NIRB_KLEOX              Reviewed;         957 AA.
AC   Q06458;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=Nitrite reductase [NAD(P)H] large subunit;
DE            EC=1.7.1.4;
GN   Name=nasB;
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M5a1;
RX   MEDLINE=93224460; PubMed=8468296;
RA   Lin J.T., Goldman B.S., Stewart V.;
RT   "Structures of genes nasA and nasB, encoding assimilatory nitrate and
RT   nitrite reductases in Klebsiella pneumoniae M5al.";
RL   J. Bacteriol. 175:2370-2378(1993).
CC   -!- CATALYTIC ACTIVITY: Ammonium hydroxide + 3 NAD(P)(+) + H(2)O =
CC       nitrite + 3 NAD(P)H.
CC   -!- COFACTOR: Binds 1 siroheme per subunit.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC   -!- SUBUNIT: Homodimer which associates with nirD (By similarity).
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S
CC       domain family.
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DR   EMBL; L06800; AAA25099.1; -; Genomic_DNA.
DR   BRENDA; 1.7.1.4; 81705.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR007419; BFD_Fer2_bd.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR006066; Nir_Si_BS.
DR   InterPro; IPR006067; Nir_Sir_4Fe4S.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR012744; Nitri_red_NirB.
DR   InterPro; IPR012748; Nitri_red_NirD.
DR   InterPro; IPR017881; Nitrite_Rdtase_lsu_NirD_bac.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   Gene3D; G3DSA:2.102.10.10; Rieske_reg; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00397; SIROHAEM.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR02378; nirD_assim_sml; 1.
DR   TIGRFAMs; TIGR02374; nitri_red_nirB; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
DR   PROSITE; PS51300; NIRD; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; FAD; Flavoprotein; Heme; Iron; Iron-sulfur; Metal-binding;
KW   NADP; Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    957       Nitrite reductase [NAD(P)H] large
FT                                subunit.
FT                                /FTId=PRO_0000199963.
FT   NP_BIND      44     79       FAD (Potential).
FT   NP_BIND     193    225       NAD or NADP (Potential).
FT   METAL       639    639       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       645    645       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       679    679       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       683    683       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       683    683       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   957 AA;  104227 MW;  A136CC7FA28C6631 CRC64;
     MTKPVLVLVG HGMVGHHFLE QCVSRDLHQQ YRIVVFCEER YAAYDRVHLT EYFAGRSAES
     LSLVEGDFFT QHGIELRLSE SVASIDREAR VVRDAFGHET HWDKLVLATG SYPFVPPVPG
     HNLEGCFVYR TLDDLDQIAA RAATARRGVV IGGGLLGLEA ANALKQLGLE THVVEFAPNL
     MAVQLDNGGA AMLREKISEL GVGVHTSKAT TEIVRNEQGL QLNFRDGSSL ATDMLVFSAG
     IRPQDALARS GGLSVGERGG ICIDNQCRTS DPDVLAIGEC ALWENKIYGL VAPGYQMAAR
     RAATLAGEAG SFSGADMSTK LKLLGVDVAS FGDAQGRTPG CQSYQWTHGP QQVYKKIVVS
     ADGKNLLGGV LVGDAGDYAT LLQMMLNGMA LPKHPESLIL PALEGSRPKA LGVAALPDGA
     QICSCHNVSK GDICQAVSGG AGDMAAIKSR TKAATGCGGC SALVKQVMEY QLAEQGVEVK
     KDICEHFPWS RQEIYHLVRV NHIRTFEQLI ARYGQGHGCE VCKPLVASVL ASCWNEYLLK
     PAHLPLQDTN DRYFANIQKD GTYSVVPRMA AGEVTPDGLI AIGQIAKRYQ LYSKVTGGQR
     IDLFGARLEQ LPAIWRELAE AGFETGHAYG KSLRTVKSCV GSTWCRYGVQ DSTGLAVTLE
     HRYKGLRAPH KIKMAVSGCT RECAEAQGKD IGVIATEKGW NLYVCGNGGM KPRHADLFAS
     DLDEATLIRS IDRLLMFYIR TADRLQRTST WMDNLEGGVD YLREMILEDS LGIGEELEQE
     MARVVESYQC EWQTTLNDPQ RLALFRSYVN SDEPDETVQR QTLRGQPQLA PFAAQGEPAL
     PSRPWQAICD LDAIPQQAGI GARLGERQIA LFRFGDQVYA LDNLEPGSEA NVLSRGLLGD
     AGGEPIVISP LYKQRIRLRD GRQCDGGEQA VRAWPVKVEN GKVWVGNQQL LARAEAS
//