ID V9EM89_PHYPR Unreviewed; 542 AA.
AC V9EM89;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Propionyl-CoA carboxylase beta chain, mitochondrial {ECO:0000313|EMBL:ETI40344.1};
GN ORFNames=F443_14242 {ECO:0000313|EMBL:ETI40344.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI40344.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI40344.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI40344.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC carboxyl carrier protein, biotin carboxylase and 2 subunits each of
CC ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
CC {ECO:0000256|ARBA:ARBA00011842}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETI40344.1}.
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DR EMBL; ANIZ01002465; ETI40344.1; -; Genomic_DNA.
DR AlphaFoldDB; V9EM89; -.
DR EnsemblProtists; ETI40344; ETI40344; F443_14242.
DR eggNOG; KOG0540; Eukaryota.
DR HOGENOM; CLU_018822_6_0_1; -.
DR OrthoDB; 864at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR PANTHER; PTHR43842:SF2; BIOTIN-DEPENDENT ACETYL-_PROPIONYL-COENZYME A CARBOXYLASE BETA5 SUBUNIT; 1.
DR PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000018721}.
FT DOMAIN 38..294
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 298..536
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 289..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 59912 MW; 0F27D3AD5638E742 CRC64;
MLAARRLRVL RQPLLQTRWM SALVDEAASP ILTPAARKLA FKEELEQARK RALEGGGAER
VAKQHEKGKL TARERIELLL DKGTFREYDM LKSHRCSDFG MEKQQYPGDG VVTGRGLING
RLTFVFSQDF TVFGGSLSET YAEKIVKIMQ KAMELGAPVI GLNDSGGARI QEGVASLAGY
ADIFQLNVLA SGVIPQLTMV MGPCAGGAVY SPAMTDYIFM CRDSSYMFVT GPDVVKTVTN
EEVTQEELGG AATHTKTSGV AHCAFDNDVE AIREMRRFFD FLPLNNKEKP PVRTSDDDRN
RPVPTLESIV PPDPNVPYNM KDIIHQIVDS FDFFEIMPDY AKNIIVGFGR MEGRVVGILA
NQPMELAGCL DINSSVKGAR FVRFCDAFNI PIVTLVDVPG FLPGTDQEYG GIIRHGAKLL
YAYAEATVPK ITIITRKAYG GAYDVMSSKH LRGDINYAWP SAEIAVMGAK GAVEIIFRGQ
NVEENTADYE KKFANPMVAA QRGFVDDIIE PVNTRRHICE DLDVLETKDV KNPWKKHGNI
PL
//