ID A0A1I2HPQ3_9ACTN Unreviewed; 860 AA.
AC A0A1I2HPQ3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Assimilatory nitrate reductase catalytic subunit {ECO:0000313|EMBL:SFF32114.1};
GN ORFNames=SAMN05216574_111129 {ECO:0000313|EMBL:SFF32114.1};
OS Blastococcus sp. DSM 46838.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1798228 {ECO:0000313|EMBL:SFF32114.1, ECO:0000313|Proteomes:UP000198589};
RN [1] {ECO:0000313|Proteomes:UP000198589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46838 {ECO:0000313|Proteomes:UP000198589};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; FOND01000011; SFF32114.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2HPQ3; -.
DR STRING; 1798228.SAMN05216574_111129; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000198589; Unassembled WGS sequence.
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:InterPro.
DR CDD; cd00508; MopB_CT_Fdh-Nap-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; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 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; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000198589}.
FT DOMAIN 16..68
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|SMART:SM00926"
FT REGION 708..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..733
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 91634 MW; 9EF8C7B81492FCD1 CRC64;
MPAAVPQSAS RGLGGTQTTR THCPYCSLQC GLDVTAGDRP ATLVPADFPT NRGGLCSKGW
SSVELLDHPE RLLRPLVRGT PGDRTSPLVE ATWDDALGRL VDAIRATQAR HGRDAVGCFG
GGSLTNEQAY QFGKFARVAL RTSAVDYNGR FCMSSAAGAA NRAFGLDRGM PFPLADIAEA
DVVVLVGSNP ADTMPPAMQY FDAGRERGAQ HVVVDPRRTA TARNAALHLQ PLPGTDLALA
NGLLHIAVAE GLVDEAYVAG RTTGFDEVRA GVAAYWPDRV ERLTGVPVAD QRRTVFALAR
AERAIVLTAR GAEQHRSGTD TASAWINLAL ALGLPGRPGS GWGTVTGQGN GQGGREHGQK
ADQLPGYRSL TDPAARAHVA AVWGVDPGDL PMPGRSAFEL LDALGTEGGV RTLLVLASNV
AVSAPDARRV ISRLGDLDFL AVSDFFLSET AELADVVLPS AMWAEEDGTM TNLEGRVIRR
RKALDPPSGV PDDLRLLATL ADRLGAGRHF SGDPETVFEE LRRASAGGTA DYSGISYRRI
DDEQGVFWPC PDEGHPGTPR LFAERFATAD GRARFVRVEH VDAAERPDAD YPYVLTTGRV
LAQYQSGTQT RRTRSLQLVA PTPRAELHPD LARRLGIGPD DVVELTTRRG RARFHALVTD
TIRPDVVFAP FHWGGGSSAN ALTDAALDPT SRMPAFKVCA VAVARADGPA ESIPPPAAAT
QPRPQPHTPP STLEPRHPAR RRSTRMKSTP RFLQGVFPIT GDGLTKPGPV DPALRYTVPH
GTSAQALYFR GGNSTGELVY VLLVRDGEPM RWFPIGARGE VHVPLRVVED LPGGTVVELH
AAAPEGVTGE LVVDLGLVEV
//
