ACPM_DICDI
ID ACPM_DICDI Reviewed; 120 AA.
AC Q54E22;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Acyl carrier protein, mitochondrial;
DE Short=ACP;
DE AltName: Full=NADH-ubiquinone oxidoreductase subunit AB1;
DE Flags: Precursor;
GN Name=ndufab1; ORFNames=DDB_G0291866;
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: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis. May be involved in the synthesis of very-long-chain fatty
CC acids. Accessory and non-catalytic subunit of the mitochondrial
CC membrane respiratory chain NADH dehydrogenase (Complex I), which
CC functions in the transfer of electrons from NADH to the respiratory
CC chain (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Complex I is composed of about 45 different subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of apo-ACP by acpS. This modification is essential for activity because
CC fatty acids are bound in thioester linkage to the sulfhydryl of the
CC prosthetic group (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000186; EAL61463.1; -; Genomic_DNA.
DR RefSeq; XP_629874.1; XM_629872.1.
DR AlphaFoldDB; Q54E22; -.
DR SMR; Q54E22; -.
DR STRING; 44689.DDB0238774; -.
DR PaxDb; Q54E22; -.
DR EnsemblProtists; EAL61463; EAL61463; DDB_G0291866.
DR GeneID; 8628372; -.
DR KEGG; ddi:DDB_G0291866; -.
DR dictyBase; DDB_G0291866; ndufab1.
DR eggNOG; KOG1748; Eukaryota.
DR HOGENOM; CLU_108696_0_0_1; -.
DR InParanoid; Q54E22; -.
DR OMA; CAETISY; -.
DR PhylomeDB; Q54E22; -.
DR Reactome; R-DDI-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-DDI-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q54E22; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 1.
DR HAMAP; MF_01217; Acyl_carrier; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR003231; Acyl_carrier.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR PANTHER; PTHR20863; PTHR20863; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Electron transport; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Mitochondrion; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Respiratory chain; Transit peptide;
KW Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..120
FT /note="Acyl carrier protein, mitochondrial"
FT /id="PRO_0000328096"
FT DOMAIN 43..117
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 77
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 120 AA; 13196 MW; 82102B70D9A6CB01 CRC64;
MIRNTFKLVS NIAVRPAFSS TFVRQPIVAS SMMVRNYGSI SEKEITDRVI GVVSQYDKVS
GKTVTPTTTF KELGLDSLDS ADILVAVEEE FGIEIPDEEA DKITSCAETI SYLRKTPTAK
