ID A1VPP4_POLNA Unreviewed; 371 AA.
AC A1VPP4;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Electron transfer flavoprotein beta-subunit {ECO:0000313|EMBL:ABM37622.1};
GN OrderedLocusNames=Pnap_2314 {ECO:0000313|EMBL:ABM37622.1};
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM37622.1, ECO:0000313|Proteomes:UP000000644};
RN [1] {ECO:0000313|Proteomes:UP000000644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644};
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000089-1};
CC Note=Binds 1 FAD per dimer. {ECO:0000256|PIRSR:PIRSR000089-1};
CC -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC {ECO:0000256|ARBA:ARBA00005817}.
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DR EMBL; CP000529; ABM37622.1; -; Genomic_DNA.
DR RefSeq; WP_011801700.1; NC_008781.1.
DR AlphaFoldDB; A1VPP4; -.
DR STRING; 365044.Pnap_2314; -.
DR KEGG; pna:Pnap_2314; -.
DR eggNOG; COG2025; Bacteria.
DR HOGENOM; CLU_034178_0_1_4; -.
DR OrthoDB; 9770286at2; -.
DR Proteomes; UP000000644; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR CDD; cd01715; ETF_alpha; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR014730; ETF_a/b_N.
DR InterPro; IPR001308; ETF_a/FixB.
DR InterPro; IPR033947; ETF_alpha_N.
DR InterPro; IPR014731; ETF_asu_C.
DR InterPro; IPR018206; ETF_asu_C_CS.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR43153; ELECTRON TRANSFER FLAVOPROTEIN ALPHA; 1.
DR PANTHER; PTHR43153:SF1; ELECTRON TRANSFER FLAVOPROTEIN SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF01012; ETF; 1.
DR Pfam; PF00766; ETF_alpha; 1.
DR PIRSF; PIRSF000089; Electra_flavoP_a; 1.
DR SMART; SM00893; ETF; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR PROSITE; PS00696; ETF_ALPHA; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000089-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000000644};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 35..227
FT /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00893"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 277..278
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 291..295
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 308..315
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 329
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ SEQUENCE 371 AA; 39782 MW; B5327550DF5BE19D CRC64;
MSQAPTPAAA PAKRPAGRGG RNLELSDELK AYKGVWVFIE HDRGHVHSVS WELIGEARKL
ADTLGCPVSA ILLGGPDEPL EKFAAEAFTF GADKAYIMKD PVLKGYRNEP FTKGMTDLVN
KYQPEIFLLG ATSMGRDLAG SVATTLLTGL TADCTELKID PTSKALAATR PTFGGSLYCT
IMTLAYRPQM ATVRPRVMLM PRADASRTGE ITYDTLGMIE TDIVTKMLDF IADANSNKIN
LPYADVIVSG GKGLKNPENF KLVFELARVL GGEVGSTRPC VQAGWVEADR QVGQTGKTVR
PKLYIAAGIS GAIQHRVGCE AADVIVAINT DVNAPIFEFA HYGIVGNAMQ VLPALTQAFA
AHLALRSRQV A
//
