ID A0A4R1HAM9_9GAMM Unreviewed; 726 AA.
AC A0A4R1HAM9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Nitrate reductase (Quinol-dependent) catalytic subunit {ECO:0000313|EMBL:TCK17641.1};
GN ORFNames=DFR30_0876 {ECO:0000313|EMBL:TCK17641.1};
OS Thiogranum longum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thiogranum.
OX NCBI_TaxID=1537524 {ECO:0000313|EMBL:TCK17641.1, ECO:0000313|Proteomes:UP000295707};
RN [1] {ECO:0000313|EMBL:TCK17641.1, ECO:0000313|Proteomes:UP000295707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19610 {ECO:0000313|EMBL:TCK17641.1,
RC ECO:0000313|Proteomes:UP000295707};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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:TCK17641.1}.
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DR EMBL; SMFX01000001; TCK17641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R1HAM9; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000295707; 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; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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 PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 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 PIRSF; PIRSF000144; CbbBc; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000295707}.
FT DOMAIN 19..76
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 726 AA; 81452 MW; 4D66F9C1C9B729D5 CRC64;
MLFGRHKKNP IKLADKGAVE WKYTTCGYCS TGCAIEVGLN KDGKAVSARG VGDADVNRGK
LCIKGIFEYE LFESGGRGRV PLMRDRIHEP FREANWDQAM DKTASEIQRI QEAHGRDAFA
IVSTGQIMTE EFYTLGKLAR GVVGTNNYDG NTTLCMASAV SGYKRSFGSD GPPGCYDDFE
HTDCLLAIGS NLPEQHPIIY WRMREAREKR PFPLIVVDPR VTMLAQNADM HLPISPGTDL
VLLNSLAYVI LEEGLQDEDY IRAHTTDFEA FKATVQDYDP LTASKLCGID EDTIRNVARV
YAKASSAMTI WTMGINQSTH GSDGVVAINN LNLITGNIGK PGGSSLSITG QCNAMGTREW
SSCSGLPGYR ALEKPQDRKD IAEFWGIDED FFPEKRGLFM TDILPAIETG QIKGLWLIAT
NPMTSMPNTA RIRKTLEKLD FLVVQDAYAD VETNEYSHVF LPAAIWAEKE GVFTNTERRV
NLIRNVMPPF GDSKPDFWIF NEMAKRIERD KKPNFPETTE QAFEEMKQLS KGRLLDISGM
SYDKIEEKRG LQWPCRDGDE TGSQRLYTDG VFQYPDGKAK LIPLPFVDNN ERPDDEYPLW
LNSGRVVEHF HTRTRTGKVG NQNKFSPTPY MEMNPDAAAE FGVEHGQYAR LVSRRGDAVV
LVQSTQRVPR NMIFVPFHYH ECVNRVSLGL LDPHSRQPAY KQCAVRVEPI EDQQAAAELN
LAARAY
//
