ID E3HY20_ACHXA Unreviewed; 309 AA.
AC E3HY20;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Electron transfer flavoprotein subunit alpha 3 {ECO:0000313|EMBL:ADP19974.1};
GN OrderedLocusNames=AXYL_06690 {ECO:0000313|EMBL:ADP19974.1};
OS Achromobacter xylosoxidans (strain A8).
OG Plasmid pA82 {ECO:0000313|EMBL:ADP19974.1,
OG ECO:0000313|Proteomes:UP000006876}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP19974.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|Proteomes:UP000006876};
RC PLASMID=pA82 {ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
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; CP002289; ADP19974.1; -; Genomic_DNA.
DR RefSeq; WP_013397162.1; NC_014642.1.
DR AlphaFoldDB; E3HY20; -.
DR KEGG; axy:AXYL_06690; -.
DR PATRIC; fig|762376.5.peg.6684; -.
DR eggNOG; COG2025; Bacteria.
DR HOGENOM; CLU_034178_0_0_4; -.
DR OrthoDB; 9770286at2; -.
DR Proteomes; UP000006876; Plasmid pA82.
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 Plasmid {ECO:0000313|EMBL:ADP19974.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 3..182
FT /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00893"
FT BINDING 202
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 227..228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 241..245
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 258..265
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ SEQUENCE 309 AA; 30916 MW; D9011ABD356B21A3 CRC64;
MTTLVIAEHD NAQLKGATLN AVAAAAKIGG DVHVLVAGAN ARAVADQAAQ AAGVAKVLLA
DAPQLADGLA ENLEAQVLAV ASGYSHILFP ATASGKNVAP RVAAKLDVAQ ISDIIGVESA
DTFQRPIYAG NAIATVQSAD AVKVITVRTT GFDAVAAQGG SAAVEEIAAV ADSGLSSFVG
REVAKSDRPE LAGARVVVSG GRGLGSAENF KILDPLADKL GAALGASRAA VDAGYAPNDW
QVGQTGKIVA PQLYVAVGIS GAIQHLAGMK DSKVIVAINK DPEAPIFGVA DYGLEGDLFQ
VVPELAGAL
//