ID G8TEW8_NIAKG Unreviewed; 1202 AA.
AC G8TEW8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Nitrate reductase., Nitrite reductase (NAD(P)H) {ECO:0000313|EMBL:AEW01556.1};
DE EC=1.7.1.4 {ECO:0000313|EMBL:AEW01556.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:AEW01556.1};
GN OrderedLocusNames=Niako_5319 {ECO:0000313|EMBL:AEW01556.1};
OS Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS GR20-10).
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=700598 {ECO:0000313|EMBL:AEW01556.1, ECO:0000313|Proteomes:UP000005438};
RN [1] {ECO:0000313|EMBL:AEW01556.1, ECO:0000313|Proteomes:UP000005438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10
RC {ECO:0000313|Proteomes:UP000005438};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Davenport K.,
RA Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Niastella koreensis GR20-10.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747}.
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DR EMBL; CP003178; AEW01556.1; -; Genomic_DNA.
DR AlphaFoldDB; G8TEW8; -.
DR STRING; 700598.Niako_5319; -.
DR KEGG; nko:Niako_5319; -.
DR PATRIC; fig|700598.3.peg.5444; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_000422_13_2_10; -.
DR Proteomes; UP000005438; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-EC.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
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; 3.30.390.30; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
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; IPR041575; Rubredoxin_C.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
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.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AEW01556.1}.
FT DOMAIN 36..92
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1202 AA; 133347 MW; 0515087F0A1B681A CRC64;
MSNVEGKENI GLYFGIQNSA FNIQHFKSMS MNNQHSGSAT TTCSYCGVGC GIVVNKDKKG
NITVEGDKNH PVNRGMLCSK GMNLHYTVND KSDRLLYPQM RYNKNMPLQR VSWDEALDRT
AAVFRTFIDK FGPDSVAFYV SGQCLTEEYY VINKLIKGFI GSNNIDTNSR LCMSSAVAGY
KMALGEDSVP GCYDDIELAD CFFITGANPA WCHPILWRRI EAHKAANPHV KIIVADPRKT
DTCSLADVHL QLNPGTDITL NHAIGRLLIE NGDVDLDFVK NHAEGYEQYK KIVFQRTLDE
AAAICGIDKA LIILAAQHIG NAKGFMSLWT MGLNQSAVGV NKNLSLINLN LITGHIGKPG
SGPFSLTGQP NAMGGREVGG LSNMLPAHRD LANPEHRSAI EKFWGGKQLS PKPGLTATEM
FDALNEGKLK AIWIICTNPL ISLPNVRVAE EGLKKAKFVV VQDMSNKPET LKYADVILPA
ASWTEKEGTM TNSERRISYL NKIVDAPGEA LPDAEIICRF AKKMGYHGFD FENASAIYDE
HAQLTEGTNI DISGLNYSVL QNRRSVQWPY PKGETGQGTV RLFTDKTFYT PSTKAVIHPV
PDENTSEKPD GDFPFILTTG RIRDQWHTMS KTGKVNKLKQ HISQSFLEIH PDDARRLHLK
DGDIAVVSSR QGEVRVKAQV SATIKPGVVF IPMHWGKILN SDLNRANNVT SAMVDPISKE
PDFKFCAVQV APYKKPRQRI VIIGAGAGAF GFVKSYREMN KEDELVIFSK ENFPFYNRVM
LPDYISGTQN WEQLIKMKES EEPGYNIKLY KGVSIEKIDR ENKCVVDSTG RTTYYDVLLM
ATGSRAAMPR NVPSLKGIFT MRSRTDADEF KNHVPSDGHV VIVGGGLLGL ELAASLREVG
IKVTIIQRIS RFLDRQLDPL GSQFLHEEMV DQNCDIYYDD EVQLFYGRTE LTGIRLKSGK
VIDCNALVFA IGTVPNIELA KETGLHCQRG VIVNERLQTS DPNVFAIGEI AEFEGVLYGI
TAAAEQQAHV VARYLQGDIA SYYKGSLFMN IIKIHGFDLC SIGIPECPND DYEEIIFLDK
AKRYYKKCII HQDRLVGAIL IGDKSEFQEF RELIANKIEL NEKRLQLLRS GKKAEPVLGR
LVCSCNNVGS ENLKNKINEG CTDFKQLCSS TGAGTGCGSC RPEVQRILEE TLAGVTSNVL
AK
//
