ID A0A126ZYF5_9MICC Unreviewed; 783 AA.
AC A0A126ZYF5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Nitrite reductase {ECO:0000313|EMBL:AMM32208.1};
GN ORFNames=SA2016_1531 {ECO:0000313|EMBL:AMM32208.1};
OS Sinomonas atrocyanea.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Sinomonas.
OX NCBI_TaxID=37927 {ECO:0000313|EMBL:AMM32208.1, ECO:0000313|Proteomes:UP000070134};
RN [1] {ECO:0000313|EMBL:AMM32208.1, ECO:0000313|Proteomes:UP000070134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 3377 {ECO:0000313|EMBL:AMM32208.1,
RC ECO:0000313|Proteomes:UP000070134};
RA Kim K.M.;
RT "Complete genome of Sinomonas atrocyanea KCTC 3377.";
RL Submitted (FEB-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; CP014518; AMM32208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A126ZYF5; -.
DR STRING; 37927.SA2016_1531; -.
DR KEGG; satk:SA2016_1531; -.
DR PATRIC; fig|37927.3.peg.1579; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000070134; Chromosome.
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 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.
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:UP000070134}.
FT DOMAIN 7..64
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 343..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..776
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 81214 MW; 13DB34C5DC773C22 CRC64;
MSQATAGPAV PTHCPYCALQ CAMSLSTPGT ASTVPEVAGR DFPTNRGGLC RKGWTSAELL
AHPGRLTEPL MRADDGGLRP VSWDAALKRV AAEVRRAQAR HGKDAVGVFG GGGLTNEKAY
LLGKFARIAL GTSRIDYNGR FCMSSAAAAG SRAFGLDRGL PFPVADLAGA DTVLLLGSNV
AETMPPFVAH LAGARAAGGL IVVDPRRSAT AALTDDGAGL HLQPAPHTDL VLLLGLAHVV
LAEGLAARDY LAERVAAAAP GEGPEALARS VAPWWPERVQ AATGVPATLL RETARRLAHS
ARTGSCYILT GRGVEQHADG TDTATAAINL ALLLGLPGSP RGGYGTLTGQ GNGQGGREHG
QKSDQLPGYR KITDPAARAH LARVWGVPEA SIPGPGLPAV ELLASLGKPA SEDPVGQKNA
GGVRCLFVHG ANLVVSAPDA TAVRAALRSL DFLVVCDFFL SETAREADLV LPVLQWAEEE
GTMTNLEGRV LRRRRAAEPP AGARSELWIM HRLAALLGAP SAFPDDPRAV FEELRAASAG
GPADYSGITY ERLDAGEALH WPCPAAPEGA GSESAAPEGA GSPGTPRLFL ERFAHPDGRA
RIVPVRPLTP AGAEAGAATP RDPSLFQLAT GRLLEHYQSG AQTRRVASLA AARPEASLDI
HPASAARLGI ADGAWVTVRR AGPTASGPRT GAPEVRCRAR LTSEVRPDTV FVPFHFPGTA
TANRVTEQRT DPISGMPEFK TTSVLVAPLP RDAPQPGTTV TAAPPAPTPV PVPVPVPSRE
ASR
//