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Database: UniProt
Entry: A0A1V2ES30_9SPHN
LinkDB: A0A1V2ES30_9SPHN
Original site: A0A1V2ES30_9SPHN 
ID   A0A1V2ES30_9SPHN        Unreviewed;       830 AA.
AC   A0A1V2ES30;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Nitrite reductase {ECO:0000313|EMBL:ONF95098.1};
DE            EC=1.7.1.4 {ECO:0000313|EMBL:ONF95098.1};
GN   Name=nasD {ECO:0000313|EMBL:ONF95098.1};
GN   ORFNames=SPHI_27280 {ECO:0000313|EMBL:ONF95098.1};
OS   Sphingomonas jeddahensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1915074 {ECO:0000313|EMBL:ONF95098.1, ECO:0000313|Proteomes:UP000188729};
RN   [1] {ECO:0000313|EMBL:ONF95098.1, ECO:0000313|Proteomes:UP000188729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G39 {ECO:0000313|EMBL:ONF95098.1,
RC   ECO:0000313|Proteomes:UP000188729};
RA   Poehlein A., Wuebbeler J.H., Steinbuechel A., Daniel R.;
RT   "Genome sequence of Sphingomonas jeddahensis G39.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRNR:PIRNR037149};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC         Evidence={ECO:0000256|ARBA:ARBA00001929};
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC       {ECO:0000256|ARBA:ARBA00005096}.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000256|ARBA:ARBA00010429}.
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:ONF95098.1}.
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DR   EMBL; MPSB01000016; ONF95098.1; -; Genomic_DNA.
DR   RefSeq; WP_076745488.1; NZ_MPSB01000016.1.
DR   AlphaFoldDB; A0A1V2ES30; -.
DR   STRING; 1915074.SPHI_27280; -.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000188729; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd19944; NirB_Fer2_BFD-like_2; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR   Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 1.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
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; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR012744; Nitri_red_NirB.
DR   InterPro; IPR017121; Nitrite_Rdtase_lsu.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   InterPro; IPR041575; Rubredoxin_C.
DR   NCBIfam; TIGR02374; nitri_red_nirB; 1.
DR   PANTHER; PTHR43809; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR   PANTHER; PTHR43809:SF1; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR   Pfam; PF04324; Fer2_BFD; 2.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF18267; Rubredoxin_C; 1.
DR   PIRSF; PIRSF037149; NirB; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR037149};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR037149}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063,
KW   ECO:0000256|PIRNR:PIRNR037149};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ONF95098.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188729}.
FT   DOMAIN          16..291
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          327..392
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          432..478
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          493..542
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          568..632
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          641..770
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
FT   REGION          805..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   830 AA;  89136 MW;  FE307F78C45CD3D2 CRC64;
     MKHEPIRVAE ADKRPHLIVI GNGMAGCRAV EELLARDPAR YRVTIVGAER HVNYNRIMLS
     PVLAGEKTFD DIVINGRDWY DSNGITLIAG DPIVAIDRAA RTVTSRGGIV MHYDRLLIAT
     GSDPFIIPVP GKDLTGVISF RDMTDVDAML AAAEKGGSAV VIGGGLLGLE AAHGLSLRGM
     TVTVIHLMPT LMERQLDEAA GWLLKTALEA RGQTIMTGAD TAEIVGDGRV EAVRLKDGTE
     IPADLVVMAV GIRPSVALAR EAGLEVGRGI KVDDHMVTSD PAILAVGECV EHQGQVYGLV
     APLWDMCRAL ADGLVDAPSG YTPAPTSTKL KVAGLDVFSA GDFSGGDGAE DIVLRDASRG
     IYKRVVVKED RIVGAVLYGD TADGNWYFDL LRRAESVADI REALIFGQAF ATGGALADPK
     AAVAALSEEA EICGCNGVSK GQVAACISMG AHSLDAVRAA CKASASCGSC TGIVEILLAL
     TLGGEVEAGP KTMCKCTSFG HDDVRREIVA QGMRSIPEVM QKLHWTTPDG CSSCRPALNY
     YLLCALPGDY VDDQQSRFVN ERMHANIQKD GTYSVVPRMW GGLTNPRELR AIADVVEKFN
     APMVKVTGGQ RLDIFGIRKE DLPAVWADLN AAGMVSGHAY GKSLRTVKTC VGSEWCRFGT
     QDSTGLGVKL ERATWGSWMP HKFKIAVSGC PRNCAEATIK DFGVVCVDSG YELHVGGNGG
     IKVRATDLLC KVATEAEAME MCAAFIQLYR EEARYLERTA PWIERVGLPY IQARLLPDAA
     ARAELARRFF FSQQFSQDDP WAARVEGGER EQHAPMARFE PVAARQEEMA
//
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