ID A0A3S1AMY5_9BACL Unreviewed; 689 AA.
AC A0A3S1AMY5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Nitrite reductase {ECO:0000313|EMBL:RUS45597.1};
GN ORFNames=ELR57_18885 {ECO:0000313|EMBL:RUS45597.1};
OS Cohnella sp. AR92.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=648716 {ECO:0000313|EMBL:RUS45597.1, ECO:0000313|Proteomes:UP000267180};
RN [1] {ECO:0000313|EMBL:RUS45597.1, ECO:0000313|Proteomes:UP000267180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR92 {ECO:0000313|EMBL:RUS45597.1,
RC ECO:0000313|Proteomes:UP000267180};
RX PubMed=29166641; DOI=10.1159/000480541;
RA Pisa J.H., Manfredi A.P., Perotti N.I., Romero H.G., Breccia J.D.,
RA Martinez M.A.;
RT "Agrowastes as Feedstock for the Production of Endo-?-Xylanase from
RT Cohnella sp. Strain AR92.";
RL J. Mol. Microbiol. Biotechnol. 27:277-288(2017).
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 -!- 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:RUS45597.1}.
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DR EMBL; RZJR01000011; RUS45597.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S1AMY5; -.
DR OrthoDB; 9805142at2; -.
DR Proteomes; UP000267180; 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 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; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
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.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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:UP000267180}.
FT DOMAIN 1..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 689 AA; 76082 MW; 59123FFBCC25FADB CRC64;
MSTQCPFCSV QCKMNVIPET LPSGRLSYRA EGKKNAASEG RLCVKGMNAH QHALSRERIL
YPLAKKDGEF VRISWEEAVD TIAERLGTIQ REHGRDAVGV YGGGSLTNES AYLLGKFARV
ALGTRYIDYN GRFCMSAAAS AGVKAFGIDR GLTNRLSEIP ETDCLLLVGT NIAECQPTLM
PYFNKAKENG TYIIVVDPRE TGTTAIADLH LKVRPGTDAA LANGLLKVLL EERLEDRLFL
RERTNGFEDV EAHLERVRLE DISELTGIDE VSIRKAAIAY GRAATGMIFT ARGVEQHRDG
HMAVRAYLNL VLATGKIGRP GCGYGAVTGQ GNGQGGREHG QKADQLPGYR LIENPADREY
VAGVWGVDPA ELPGKGVSAY EMMELTISRD IRGMLVMGSN PIVSNPNAGA VEEGLKSLEF
LAVADMFLSE TAELADIVLP VTSYLENEGT LTNLEGRVLL REAARPVPGE ARHDWQWLCD
LAERWGRKEK FSYFHAEEIF EELRIASRGG VADYYGITYE RLRKEEGIYW PCPDLDHPGM
KRLFEERFAH SDGKAQLIAV GSLSPGEEAD GDYPLLMTNG RLLPHYLTGV QTRRSPALSA
RAIENVVEIH PSTARRYRVE DGALVRIHSR RGTAVLRSKV TNGIREDTLF IPMHWGGVQN
VNLLTNPLLD PVCRMPDFKV SAVRIEPWS
//
