AIFB_DICDI
ID AIFB_DICDI Reviewed; 387 AA.
AC Q54NS8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Apoptosis-inducing factor homolog B;
DE EC=1.-.-.-;
GN Name=aifB; ORFNames=DDB_G0285005;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Putative FAD-dependent oxidoreductase. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000073; EAL64966.1; -; Genomic_DNA.
DR RefSeq; XP_639989.1; XM_634897.1.
DR AlphaFoldDB; Q54NS8; -.
DR SMR; Q54NS8; -.
DR STRING; 44689.DDB0266656; -.
DR PaxDb; Q54NS8; -.
DR EnsemblProtists; EAL64966; EAL64966; DDB_G0285005.
DR GeneID; 8624906; -.
DR KEGG; ddi:DDB_G0285005; -.
DR dictyBase; DDB_G0285005; aifB.
DR eggNOG; KOG2495; Eukaryota.
DR HOGENOM; CLU_019845_2_0_1; -.
DR InParanoid; Q54NS8; -.
DR OMA; CEMAGQI; -.
DR PhylomeDB; Q54NS8; -.
DR PRO; PR:Q54NS8; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..387
FT /note="Apoptosis-inducing factor homolog B"
FT /id="PRO_0000331384"
FT BINDING 12..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 292
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 387 AA; 42511 MW; 407FBD85043CD28B CRC64;
MTSEKKRVLI IGGGYGGCEV AKQLDSKFNV TVVERKQTFF HSVGSVRAVV EPELVKKIYI
PYDKLLKNGK FIFGTVIEIS PTLAKLEDGQ ELTFDYLVIA TGSNSLAPFK APLEKKSSSE
ILNYFQNFSQ QIKQAKSILI VGGGAVACEL VSEIVEKYPV KDSELVKKIT IVHSGSKLVN
PKMNDKFTNV VSKAMKKRNV EVILNDRITM PDEIKANLLN QTSPNIQISS QNYTTEKGVP
IQADLIIWTV GIKTNSESYQ SHFSNVINES GQLKVNLSCQ VQGYNNVFAI GDCTDFDEFK
TAYNAGYHAA IAAKAIDALS KGKSNDKLAK HKVSGPILSL SLGPQDGITQ ISPTMCLGSF
ATKMIKSKSL FIDRYISQLN NPKPLIQ