ID A6TT10_ALKMQ Unreviewed; 366 AA.
AC A6TT10;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Oxidoreductase FAD/NAD(P)-binding domain protein {ECO:0000313|EMBL:ABR49328.1};
GN OrderedLocusNames=Amet_3190 {ECO:0000313|EMBL:ABR49328.1};
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR49328.1, ECO:0000313|Proteomes:UP000001572};
RN [1] {ECO:0000313|Proteomes:UP000001572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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DR EMBL; CP000724; ABR49328.1; -; Genomic_DNA.
DR RefSeq; WP_012064293.1; NC_009633.1.
DR AlphaFoldDB; A6TT10; -.
DR STRING; 293826.Amet_3190; -.
DR KEGG; amt:Amet_3190; -.
DR eggNOG; COG2871; Bacteria.
DR HOGENOM; CLU_003827_7_2_9; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000001572; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06211; phenol_2-monooxygenase_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43644; NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR43644:SF1; NAD(P)H-FLAVIN REDUCTASE; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000001572}.
FT DOMAIN 35..125
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 128..234
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 366 AA; 40962 MW; ABCAA24CE863D8FC CRC64;
MNTILTTILI ITGITTTLAL LLTLANTYIA DYGERKIRIN KDKEFIVEGG NTLLSSLIEN
EIYLPSACGG KGSCGYCKCA INEGGGPVLP TELSYLTEDD MKNNVRLSCQ VKVKADMEIQ
IAEDLLNVKQ FEAIVEKTED LTSTIKLLRL KITDGQEIEF KAGQYVQLLA PPYPGSPDEV
FRAYSIASSP NNKGYIDLII GYVPDGLLTT YVHKHLSEGD EILFNGPFGD FYLQDCEEDA
ILVAVGTGMA PIRSILFEML NKKIDRNTIF FFGAKTPEDL FLLDEMTMFE KELPRFKFVP
TLSRAPEESQ WKGEEGRVTD AMMKFLEKKE GREAYLCGSA PMIDSTVKTL VERAFADNKI
YYDKFD
//
