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Protein

Nitrite reductase [NAD(P)H] large subunit

Gene

nasB

Organism
Klebsiella oxytoca
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Ammonia + 3 NAD(P)+ + 2 H2O = nitrite + 3 NAD(P)H.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: nitrate reduction (assimilation)

This protein is involved in the pathway nitrate reduction (assimilation), which is part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the pathway nitrate reduction (assimilation) and in Nitrogen metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi639 – 6391Iron-sulfur (4Fe-4S)By similarity
Metal bindingi645 – 6451Iron-sulfur (4Fe-4S)By similarity
Metal bindingi679 – 6791Iron-sulfur (4Fe-4S)By similarity
Metal bindingi683 – 6831Iron (siroheme axial ligand)By similarity
Metal bindingi683 – 6831Iron-sulfur (4Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 7936FADSequence analysisAdd
BLAST
Nucleotide bindingi193 – 22533NAD or NADPSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrate assimilation

Keywords - Ligandi

4Fe-4S, FAD, Flavoprotein, Heme, Iron, Iron-sulfur, Metal-binding, NADP

Enzyme and pathway databases

UniPathwayiUPA00653.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrite reductase [NAD(P)H] large subunit (EC:1.7.1.4)
Gene namesi
Name:nasB
OrganismiKlebsiella oxytoca
Taxonomic identifieri571 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 957957Nitrite reductase [NAD(P)H] large subunitPRO_0000199963Add
BLAST

Interactioni

Subunit structurei

Homodimer which associates with NirD.By similarity

Protein-protein interaction databases

STRINGi1006551.KOX_23110.

Structurei

3D structure databases

ProteinModelPortaliQ06458.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107QZF. Bacteria.
COG1251. LUCA.
COG2146. LUCA.

Family and domain databases

Gene3Di2.102.10.10. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR007419. BFD-like_2Fe2S-bd_dom.
IPR023753. FAD/NAD-binding_dom.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR012744. Nitri_red_NirB.
IPR012748. Nitri_red_NirD.
IPR017881. Nitrite_Rdtase_lsu_NirD_bac.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
IPR017941. Rieske_2Fe-2S.
[Graphical view]
PfamiPF04324. Fer2_BFD. 2 hits.
PF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF13806. Rieske_2. 1 hit.
[Graphical view]
PRINTSiPR00397. SIROHAEM.
SUPFAMiSSF50022. SSF50022. 1 hit.
SSF51905. SSF51905. 2 hits.
SSF55124. SSF55124. 1 hit.
TIGRFAMsiTIGR02378. nirD_assim_sml. 1 hit.
TIGR02374. nitri_red_nirB. 1 hit.
PROSITEiPS00365. NIR_SIR. 1 hit.
PS51300. NIRD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06458-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKPVLVLVG HGMVGHHFLE QCVSRDLHQQ YRIVVFCEER YAAYDRVHLT
60 70 80 90 100
EYFAGRSAES LSLVEGDFFT QHGIELRLSE SVASIDREAR VVRDAFGHET
110 120 130 140 150
HWDKLVLATG SYPFVPPVPG HNLEGCFVYR TLDDLDQIAA RAATARRGVV
160 170 180 190 200
IGGGLLGLEA ANALKQLGLE THVVEFAPNL MAVQLDNGGA AMLREKISEL
210 220 230 240 250
GVGVHTSKAT TEIVRNEQGL QLNFRDGSSL ATDMLVFSAG IRPQDALARS
260 270 280 290 300
GGLSVGERGG ICIDNQCRTS DPDVLAIGEC ALWENKIYGL VAPGYQMAAR
310 320 330 340 350
RAATLAGEAG SFSGADMSTK LKLLGVDVAS FGDAQGRTPG CQSYQWTHGP
360 370 380 390 400
QQVYKKIVVS ADGKNLLGGV LVGDAGDYAT LLQMMLNGMA LPKHPESLIL
410 420 430 440 450
PALEGSRPKA LGVAALPDGA QICSCHNVSK GDICQAVSGG AGDMAAIKSR
460 470 480 490 500
TKAATGCGGC SALVKQVMEY QLAEQGVEVK KDICEHFPWS RQEIYHLVRV
510 520 530 540 550
NHIRTFEQLI ARYGQGHGCE VCKPLVASVL ASCWNEYLLK PAHLPLQDTN
560 570 580 590 600
DRYFANIQKD GTYSVVPRMA AGEVTPDGLI AIGQIAKRYQ LYSKVTGGQR
610 620 630 640 650
IDLFGARLEQ LPAIWRELAE AGFETGHAYG KSLRTVKSCV GSTWCRYGVQ
660 670 680 690 700
DSTGLAVTLE HRYKGLRAPH KIKMAVSGCT RECAEAQGKD IGVIATEKGW
710 720 730 740 750
NLYVCGNGGM KPRHADLFAS DLDEATLIRS IDRLLMFYIR TADRLQRTST
760 770 780 790 800
WMDNLEGGVD YLREMILEDS LGIGEELEQE MARVVESYQC EWQTTLNDPQ
810 820 830 840 850
RLALFRSYVN SDEPDETVQR QTLRGQPQLA PFAAQGEPAL PSRPWQAICD
860 870 880 890 900
LDAIPQQAGI GARLGERQIA LFRFGDQVYA LDNLEPGSEA NVLSRGLLGD
910 920 930 940 950
AGGEPIVISP LYKQRIRLRD GRQCDGGEQA VRAWPVKVEN GKVWVGNQQL

LARAEAS
Length:957
Mass (Da):104,227
Last modified:October 1, 1994 - v1
Checksum:iA136CC7FA28C6631
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06800 Genomic DNA. Translation: AAA25099.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06800 Genomic DNA. Translation: AAA25099.1.

3D structure databases

ProteinModelPortaliQ06458.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1006551.KOX_23110.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107QZF. Bacteria.
COG1251. LUCA.
COG2146. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00653.

Family and domain databases

Gene3Di2.102.10.10. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR007419. BFD-like_2Fe2S-bd_dom.
IPR023753. FAD/NAD-binding_dom.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR012744. Nitri_red_NirB.
IPR012748. Nitri_red_NirD.
IPR017881. Nitrite_Rdtase_lsu_NirD_bac.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
IPR017941. Rieske_2Fe-2S.
[Graphical view]
PfamiPF04324. Fer2_BFD. 2 hits.
PF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF13806. Rieske_2. 1 hit.
[Graphical view]
PRINTSiPR00397. SIROHAEM.
SUPFAMiSSF50022. SSF50022. 1 hit.
SSF51905. SSF51905. 2 hits.
SSF55124. SSF55124. 1 hit.
TIGRFAMsiTIGR02378. nirD_assim_sml. 1 hit.
TIGR02374. nitri_red_nirB. 1 hit.
PROSITEiPS00365. NIR_SIR. 1 hit.
PS51300. NIRD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Structures of genes nasA and nasB, encoding assimilatory nitrate and nitrite reductases in Klebsiella pneumoniae M5al."
    Lin J.T., Goldman B.S., Stewart V.
    J. Bacteriol. 175:2370-2378(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: M5a1.

Entry informationi

Entry nameiNIRB_KLEOX
AccessioniPrimary (citable) accession number: Q06458
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 20, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.