ID A0A1I7DUY2_9MICC Unreviewed; 757 AA.
AC A0A1I7DUY2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Assimilatory nitrate reductase (NADH) alpha subunit apoprotein {ECO:0000313|EMBL:SFU15426.1};
GN ORFNames=SAMN04487915_11522 {ECO:0000313|EMBL:SFU15426.1};
OS Arthrobacter sp. ov118.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1761747 {ECO:0000313|EMBL:SFU15426.1, ECO:0000313|Proteomes:UP000199457};
RN [1] {ECO:0000313|EMBL:SFU15426.1, ECO:0000313|Proteomes:UP000199457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV118 {ECO:0000313|EMBL:SFU15426.1,
RC ECO:0000313|Proteomes:UP000199457};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FPAY01000015; SFU15426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7DUY2; -.
DR STRING; 1761747.SAMN04487915_11522; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000199457; Unassembled WGS sequence.
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 PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 88..521
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 630..733
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 27..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 79900 MW; 9094C04B69A7DA28 CRC64;
MTKSADTHCP YCALQCAMTL KSPAALTPAV QPGSDPVPAP PAPPAAAAAA PAPAGPLLEV
SGRDFPTNRG GLCRKGWTSA SLLSHPGRVT EPMLKDADGV HRPVSWDEAL RLITAAVKET
RDRYGADAVG VFGGGGLTNE KAYQLGKFAR LALGTSRIDY NGRFCMSSAA AAGMRAFGVD
RGLPFPLEDL DGASTILMLG SNVAETMPPF VQHLQGARDA GGLIVVDPRR SATAAFTSDG
GGLHLQPLPG TDLTLLLGLS HVVIHEGLAD TGFISTRTSG FEALARSVNA FWPERVQSLT
GVPADLIRET ARRLADGATK GGAYILTGRG VEQHIDGTDT ATAAINLSLL LGLPGSSRSG
YGTLTGQGNG QGGREHGQKA DQLPGYRKIT DPAARAHMAK VWDVPESLIP GPGLPAVQLL
KSLGQPDGVR CLFVHASNIA VASPDANAVI AGLRSLDFLV VCDFFVSETA AEADLILPVL
QWAEEEGTLT NLEGRVLRRR RALQPPAGAR SELWIMARLA ELLEAPSTYS EDPETVFEEL
RLASAGGLAD YSGIDYAILD RGEAAYWPFP AGGTGTPRLF LDAFAHADGK AVMTPVAPRR
RRPPAATPDR DSSRDISARD IPGPGAKTMT LITGRLLEHY QSGAQTRRVS ELFASQPEAK
MQIHPAAAAS MGVTDGAFVS VANERGEVLC RAELSTDIRP ETVFLPFHFP ELESANRLTE
AATDPISGMP EFKFNKVWVR VATNAQQSSV LQTSEAS
//
