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Database: UniProt
Entry: A0A2T4IBB9_9RHOO
LinkDB: A0A2T4IBB9_9RHOO
Original site: A0A2T4IBB9_9RHOO 
ID   A0A2T4IBB9_9RHOO        Unreviewed;       850 AA.
AC   A0A2T4IBB9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Periplasmic nitrate reductase {ECO:0000256|HAMAP-Rule:MF_01630};
DE            EC=1.9.6.1 {ECO:0000256|HAMAP-Rule:MF_01630};
GN   Name=napA {ECO:0000256|HAMAP-Rule:MF_01630};
GN   ORFNames=C8261_16390 {ECO:0000313|EMBL:PTD95075.1};
OS   Pseudothauera lacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Pseudothauera.
OX   NCBI_TaxID=2136175 {ECO:0000313|EMBL:PTD95075.1, ECO:0000313|Proteomes:UP000241193};
RN   [1] {ECO:0000313|EMBL:PTD95075.1, ECO:0000313|Proteomes:UP000241193}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D20 {ECO:0000313|EMBL:PTD95075.1,
RC   ECO:0000313|Proteomes:UP000241193};
RA   Keele B.F.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PTD95075.1, ECO:0000313|Proteomes:UP000241193}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D20 {ECO:0000313|EMBL:PTD95075.1,
RC   ECO:0000313|Proteomes:UP000241193};
RA   Liang Q.-Y.;
RT   "Thauera lacus sp. nov., isolated from an saline lake in Inner Mongolia,
RT   China.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalytic subunit of the periplasmic nitrate reductase
CC       complex NapAB. Receives electrons from NapB and catalyzes the reduction
CC       of nitrate to nitrite. {ECO:0000256|HAMAP-Rule:MF_01630}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome] + 2 H(+) + nitrate = 2 Fe(III)-
CC         [cytochrome] + H2O + nitrite; Xref=Rhea:RHEA:12909, Rhea:RHEA-
CC         COMP:11777, Rhea:RHEA-COMP:11778, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.6.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01630};
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|HAMAP-Rule:MF_01630};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC       bis-MGD) cofactor per subunit. {ECO:0000256|HAMAP-Rule:MF_01630};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01630};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_01630};
CC   -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC       composed of NapA and NapB. {ECO:0000256|HAMAP-Rule:MF_01630}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_01630}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000256|HAMAP-Rule:MF_01630}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/NapA/NarB subfamily.
CC       {ECO:0000256|ARBA:ARBA00008747, ECO:0000256|HAMAP-Rule:MF_01630}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01630}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PTD95075.1}.
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DR   EMBL; PZKC01000020; PTD95075.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4IBB9; -.
DR   OrthoDB; 9810782at2; -.
DR   Proteomes; UP000241193; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0050140; F:nitrate reductase (cytochrome) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR   CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.200.210; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   HAMAP; MF_01630; Nitrate_reduct_NapA; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR010051; Periplasm_NO3_reductase_lsu.
DR   InterPro; IPR006311; TAT_signal.
DR   NCBIfam; TIGR01706; NAPA; 1.
DR   PANTHER; PTHR43105:SF11; PERIPLASMIC NITRATE REDUCTASE; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01630};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW   Rule:MF_01630};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01630};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01630};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01630};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|HAMAP-
KW   Rule:MF_01630};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063, ECO:0000256|HAMAP-
KW   Rule:MF_01630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01630};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_01630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241193};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_01630};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01630}.
FT   DOMAIN          43..99
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   REGION          316..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         50
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         53
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         57
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         85
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         87
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         154
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         179
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         183
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         216..223
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         247..251
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         387
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         391
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         497
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         523..524
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         546
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         573
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         740..749
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         816
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         824
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
FT   BINDING         841
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01630"
SQ   SEQUENCE   850 AA;  95701 MW;  5C0CA25EE74B4911 CRC64;
     MTNMDRRAFI KSNAVAAAAA TAGIGGIPVV AQAQQAGNSS TRVRWDKAAC RFCGVGCSVL
     VGVQNDRVVA TQGDPDSPVN RGLNCIKGYF LSKIMYGEDR LTRPLLRMKG GKYDKNGEFS
     PVSWTQAFDI MAEKWKAALK EHGPRSVGMF GSGQWTVWEG YAASKLHKAG FRTNNIDPNA
     RHCMASAVAG FMRTFGMDEP MGCYDDIENA DAFVLWGSNM AEMHPILWSR ITDRRLTHNG
     CEVHVLSTFE HRSYELADNP MIFEPHTDLA ILNYICHHII SNNKVNRDFV AKHVKFAMGE
     GDIGFGLRPN HPLEAKATSN GYPGADGKPK GNPGAAKEMS FDEFAKYVSD YTLEKVSRLS
     RVPADRLRRM AELYADPNRK VTSFWTMGFN QHTRGTWVNN MIYNVHLLVG KISEPGNSPF
     SLTGQPSACG TAREVGTFAH RLPADMVVTN PKHREFAENI WQLPEGTIPD WVGLHAVAQS
     RALKDGVLKC YWTSTTNNMQ AGPNVNEEIY PGWRNPETFV VVSDVYPTVS ALSADLILPS
     AMWTEKEGAF GNAERRGQFW RQQVRAPGEA KSDLWQYIEF AKRFKVEEVW PAELIAKKPS
     VRGKTLYDVL YANGEVNKYP LSEVAKVNAH AWAGYMNDES RELGFYLQKG LFEEYARFTR
     GKYHDLAYFD DYHRARGLRW PVVDGKETLW RYKEGYDPYV KAGEGWNFYG HPDGRATIFA
     LPYQEPHDKP GGEYDLWMCT GRVLEHWHTG SMTRRVPELH RSVPEAQVFM HPEDASRRGL
     QRGMSVKVAS KRGEIVARLE TRGRNKPPQG LIFVPFFDEG RLVNKLIEDA TCPISKETDF
     KKCPVKVMRA
//
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