ID A0A1E4MEM8_9SPHN Unreviewed; 513 AA.
AC A0A1E4MEM8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:ODU69676.1};
GN ORFNames=ABT11_11830 {ECO:0000313|EMBL:ODU69676.1};
OS Novosphingobium sp. SCN 66-18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1660121 {ECO:0000313|EMBL:ODU69676.1, ECO:0000313|Proteomes:UP000094170};
RN [1] {ECO:0000313|EMBL:ODU69676.1, ECO:0000313|Proteomes:UP000094170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
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:ODU69676.1}.
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DR EMBL; MEGD01000020; ODU69676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4MEM8; -.
DR Proteomes; UP000094170; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR Gene3D; 3.10.20.600; -; 1.
DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 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}.
FT DOMAIN 400..445
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 513 AA; 53473 MW; 87160D602C3DFB55 CRC64;
MTVTVRISDD ALALACGADE VAAAFEKAGC TVERVSSWGM HWLEPLAEID GVGYGPLTTD
DVPAVLAGTS PLGIGPIADH PFIAPQQRFT FARAGKTRPL DLGDYATSGG WAGLRKAHDI
GAEATIAEVT ASGLRGRGGA GFPAGIKWTT VAKAKAAQKY VVCNADEGDS ATFADRMVME
GDPFMLIEGM AIAAYAVGAT RGYVYIRSEY PHAIAKMEAA VRACAHIIAP FVLEVRTGAG
AYVCGEETSL LNSLEGKRGE VRAKPPLPAL EGLFGKPTVV NNVLTLAAVP WILAHGGTAY
AAVGFGRSKG TMPIQLAGNV KHGGLFEVGF GITLGELVND IGGGTASGRP VRAVQVGGPL
GAYHPPSDFH LPFDYESFAA ADGLIGHAGL TVFDDTADMS AQARFAMAFC AAESCGKCTP
CRIGSTRGVE LIDRIRARAP RAADAVERLP QTHNARKGAR TLAEEITLLE DLCETMKFGS
LCALGGFTPY PVLSALKHWP EDFGAAVPAE AAE
//
