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Protein

Nitrite reductase

Gene

nirS

Organism
Paracoccus pantotrophus (Thiosphaera pantotropha)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+.
NH3 + H2O + acceptor = hydroxylamine + reduced acceptor.

Cofactori

hemeNote: Binds 2 heme groups per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi46Iron (heme axial ligand)1
Binding sitei94Heme (covalent)1
Binding sitei97Heme (covalent)1
Metal bindingi98Iron (heme axial ligand)1
Metal bindingi229Iron (heme D1 proximal ligand)1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.7.2.1. 4531.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrite reductase (EC:1.7.2.1)
Alternative name(s):
Cytochrome cd1
Cytochrome oxidase
Hydroxylamine reductase (EC:1.7.99.1)
Gene namesi
Name:nirS
OrganismiParacoccus pantotrophus (Thiosphaera pantotropha)
Taxonomic identifieri82367 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Add BLAST29
ChainiPRO_000000657530 – 596Nitrite reductaseAdd BLAST567

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1596
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi39 – 41Combined sources3
Helixi42 – 45Combined sources4
Beta strandi50 – 55Combined sources6
Helixi61 – 63Combined sources3
Helixi80 – 93Combined sources14
Helixi95 – 98Combined sources4
Beta strandi105 – 107Combined sources3
Helixi112 – 118Combined sources7
Helixi120 – 127Combined sources8
Turni132 – 134Combined sources3
Turni136 – 138Combined sources3
Beta strandi142 – 144Combined sources3
Helixi146 – 157Combined sources12
Helixi168 – 174Combined sources7
Beta strandi176 – 179Combined sources4
Helixi181 – 183Combined sources3
Helixi194 – 196Combined sources3
Beta strandi197 – 202Combined sources6
Turni203 – 206Combined sources4
Beta strandi207 – 212Combined sources6
Turni213 – 215Combined sources3
Beta strandi218 – 223Combined sources6
Beta strandi228 – 233Combined sources6
Beta strandi239 – 244Combined sources6
Beta strandi247 – 253Combined sources7
Beta strandi256 – 258Combined sources3
Beta strandi261 – 266Combined sources6
Beta strandi269 – 276Combined sources8
Turni283 – 285Combined sources3
Beta strandi286 – 293Combined sources8
Beta strandi296 – 301Combined sources6
Turni302 – 304Combined sources3
Beta strandi307 – 312Combined sources6
Turni318 – 320Combined sources3
Beta strandi323 – 325Combined sources3
Beta strandi329 – 334Combined sources6
Beta strandi336 – 345Combined sources10
Turni346 – 349Combined sources4
Beta strandi350 – 355Combined sources6
Beta strandi359 – 368Combined sources10
Beta strandi371 – 378Combined sources8
Beta strandi384 – 389Combined sources6
Helixi390 – 392Combined sources3
Beta strandi394 – 399Combined sources6
Turni400 – 403Combined sources4
Beta strandi404 – 410Combined sources7
Beta strandi412 – 416Combined sources5
Beta strandi422 – 426Combined sources5
Turni427 – 429Combined sources3
Beta strandi430 – 447Combined sources18
Turni450 – 452Combined sources3
Turni454 – 456Combined sources3
Beta strandi459 – 465Combined sources7
Beta strandi481 – 486Combined sources6
Helixi493 – 496Combined sources4
Beta strandi499 – 503Combined sources5
Helixi504 – 506Combined sources3
Beta strandi510 – 512Combined sources3
Beta strandi516 – 519Combined sources4
Helixi521 – 525Combined sources5
Beta strandi533 – 539Combined sources7
Beta strandi543 – 551Combined sources9
Beta strandi559 – 564Combined sources6
Turni565 – 568Combined sources4
Beta strandi569 – 574Combined sources6
Beta strandi581 – 587Combined sources7
Helixi588 – 592Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AOFX-ray2.00A/B30-596[»]
1AOMX-ray1.80A/B30-596[»]
1AOQX-ray1.80A/B30-596[»]
1DY7X-ray1.60A/B30-596[»]
1E2RX-ray1.59A/B30-596[»]
1GQ1X-ray1.40A/B30-596[»]
1H9XX-ray2.10A/B30-596[»]
1H9YX-ray2.40A/B30-596[»]
1HCMX-ray2.50A/B30-596[»]
1HJ3X-ray1.60A/B30-596[»]
1HJ4X-ray1.60A/B30-596[»]
1HJ5X-ray1.46A/B30-596[»]
1QKSX-ray1.28A/B30-596[»]
ProteinModelPortaliP72181.
SMRiP72181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP72181.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini77 – 162Cytochrome cPROSITE-ProRule annotationAdd BLAST86

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 76N-terminal tailAdd BLAST47
Regioni163 – 596D1-heme domainAdd BLAST434

Sequence similaritiesi

Contains 1 cytochrome c domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
2.130.10.10. 1 hit.
2.140.10.20. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR003143. Cyt_cd1_C.
IPR011048. Haem_d1.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF13442. Cytochrome_CBB3. 1 hit.
[Graphical view]
SUPFAMiSSF46626. SSF46626. 2 hits.
SSF51004. SSF51004. 1 hit.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P72181-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRQRTPFARP GLLASAALAL VLGPLAASAQ EQVAPPKDPA AALEDHKTRT
60 70 80 90 100
DNRYEPSLDN LAQQDVAAPG APEGVSALSD AQYNEANKIY FERCAGCHGV
110 120 130 140 150
LRKGATGKAL TPDLTRDLGF DYLQSFITYG SPAGMPNWGT SGELSAEQVD
160 170 180 190 200
LMANYLLLDP AAPPEFGMKE MRESWKVHVA PEDRPTQQEN DWDLENLFSV
210 220 230 240 250
TLRDAGQIAL IDGATYEIKS VLDTGYAVHI SRLSASGRYL FVIGRDGKVN
260 270 280 290 300
MIDLWMKEPT TVAEIKIGSE ARSIETSKME GWEDKYAIAG AYWPPQYVIM
310 320 330 340 350
DGETLEPKKI QSTRGMTYDE QEYHPEPRVA AILASHYRPE FIVNVKETGK
360 370 380 390 400
ILLVDYTDLD NLKTTEISAE RFLHDGGLDG SHRYFITAAN ARNKLVVIDT
410 420 430 440 450
KEGKLVAIED TGGQTPHPGR GANFVHPTFG PVWATSHMGD DSVALIGTDP
460 470 480 490 500
EGHPDNAWKI LDSFPALGGG SLFIKTHPNS QYLYVDATLN PEAEISGSVA
510 520 530 540 550
VFDIKAMTGD GSDPEFKTLP IAEWAGITEG QPRVVQGEFN KDGTEVWFSV
560 570 580 590
WNGKDQESAL VVVDDKTLEL KHVIKDERLV TPTGKFNVYN TMTDTY
Length:596
Mass (Da):65,383
Last modified:November 8, 2002 - v2
Checksum:iABAD0C871E8FB7F1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti28S → A in AAB17878 (PubMed:10708389).Curated1
Sequence conflicti76S → T in AAB17878 (PubMed:10708389).Curated1
Sequence conflicti130G → A in AAB17878 (PubMed:10708389).Curated1
Sequence conflicti214A → T in AAB17878 (PubMed:10708389).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75413 Genomic DNA. Translation: AAB17878.1.
AJ401462 Genomic DNA. Translation: CAC03621.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75413 Genomic DNA. Translation: AAB17878.1.
AJ401462 Genomic DNA. Translation: CAC03621.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AOFX-ray2.00A/B30-596[»]
1AOMX-ray1.80A/B30-596[»]
1AOQX-ray1.80A/B30-596[»]
1DY7X-ray1.60A/B30-596[»]
1E2RX-ray1.59A/B30-596[»]
1GQ1X-ray1.40A/B30-596[»]
1H9XX-ray2.10A/B30-596[»]
1H9YX-ray2.40A/B30-596[»]
1HCMX-ray2.50A/B30-596[»]
1HJ3X-ray1.60A/B30-596[»]
1HJ4X-ray1.60A/B30-596[»]
1HJ5X-ray1.46A/B30-596[»]
1QKSX-ray1.28A/B30-596[»]
ProteinModelPortaliP72181.
SMRiP72181.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.7.2.1. 4531.

Miscellaneous databases

EvolutionaryTraceiP72181.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
2.130.10.10. 1 hit.
2.140.10.20. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR003143. Cyt_cd1_C.
IPR011048. Haem_d1.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF13442. Cytochrome_CBB3. 1 hit.
[Graphical view]
SUPFAMiSSF46626. SSF46626. 2 hits.
SSF51004. SSF51004. 1 hit.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNIRS_PARPN
AccessioniPrimary (citable) accession number: P72181
Secondary accession number(s): Q9FCQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 8, 2002
Last modified: November 2, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.