ID A0A0C9ND20_SPHPI Unreviewed; 866 AA.
AC A0A0C9ND20;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=DNA, contig: SP632 {ECO:0000313|EMBL:GAN14197.1};
GN ORFNames=SP6_32_00040 {ECO:0000313|EMBL:GAN14197.1};
OS Sphingomonas paucimobilis NBRC 13935.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN14197.1, ECO:0000313|Proteomes:UP000032025};
RN [1] {ECO:0000313|EMBL:GAN14197.1, ECO:0000313|Proteomes:UP000032025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN14197.1,
RC ECO:0000313|Proteomes:UP000032025};
RA Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., Ohji S.,
RA Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC 13935.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:GAN14197.1}.
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DR EMBL; BBJS01000032; GAN14197.1; -; Genomic_DNA.
DR RefSeq; WP_007404696.1; NZ_BBJS01000032.1.
DR AlphaFoldDB; A0A0C9ND20; -.
DR GeneID; 78528638; -.
DR Proteomes; UP000032025; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
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; 3.40.50.740; -; 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 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; 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 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 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.
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}.
FT DOMAIN 1..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 866 AA; 93465 MW; C5AC23003FE0ECC5 CRC64;
MTPIKTTCAY CGVGCGIRAT VTGERQVWIE GDPDHPANRG KLCSKGTHLG ETVGLEGRLL
HPMIGKRRAS WDKALDLVAK RFRDTIAQHG PDSVAFYVSG QLLTEDYYLA NKLMKGFIGS
ANIDTNSRLC MSSAVVGHIR AFGEDIVPAS YEDIDAADLI VLVGSNTAWC HPIVYQRIRA
RCDAGAKLVV IDPRRTETAE HADLHLAIRP GSDVALMNGA LAWARAAGIV DEEFLAASVA
VPEDFWTALE DGSDLWSVAK TCDVAPADLR RFYELFAATP RTVTLFSQGI NQSTTGTDQV
NAILNLHLAT RRIGKPGAAP FSITGQPNAM GGREVGGLAS TLAAHMDFAP ENRARVQRFW
ASPSIAPKPG LKAVDLFREL GQGRIKALWI MATNPAVSMP DAGSVREALA TCPFVVVSDV
IAETDSSVHA HVRLPAAAWG EKDGTVTNSD RTISRQRALF PLPGEAQPDW WIIKEVGRRM
GWKTAFAYDR PAEIWREHCR LSHYENHGQR LFALPGRASG GNAEYDAMQP FRWGGTPFAD
GRFPTPDGRA RLVPVAQKAL PEPLRDWPMM LNTGRYRDHW HTMTRTGLAP KLARHREEPL
VEVHPDDAHR LNLTDGGLAR VGTPQGTSLY RVAVSPGQRP GELFVPIHWT DKTASGGRTG
LLPRPLTDPY SGQPGFKRTP ASIAAVTTRW CGFAILSGEA SAVPDCLWAT RIAVPGGWLW
EVAGDGDPAV LEAMLPKGQR IEATDPARGS RRVAVITGDH LAAVLFLTER GELPGRDWLI
AQLSTPEVAP TILAGRAPGA QVERGAIVCA CFDIGMRTIV TAIRDQQLAD VASIGAALGA
GTNCGSCRPA LARLLAETQE PAHAHG
//
