ID D3KTV3_9MONI Unreviewed; 263 AA.
AC D3KTV3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Beta subunit of acetyl-coenzyme A carboxylase {ECO:0000313|EMBL:BAI77758.1};
DE Flags: Fragment;
GN Name=accD {ECO:0000313|EMBL:BAI77758.1};
OS Hymenophyllum minimum.
OG Plastid; Chloroplast {ECO:0000313|EMBL:BAI77758.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Hymenophyllales; Hymenophyllaceae;
OC Hymenophylloideae; Hymenophyllum.
OX NCBI_TaxID=638565 {ECO:0000313|EMBL:BAI77758.1};
RN [1] {ECO:0000313|EMBL:BAI77758.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20060917; DOI=10.1016/j.ympev.2010.01.001;
RA Hennequin S., Ebihara A., Dubuisson J.-Y., Schneider H.;
RT "Chromosome number evolution in Hymenophyllum (Hymenophyllaceae), with
RT special reference to the subgenus Hymenophyllum.";
RL Mol. Phylogenet. Evol. 55:47-59(2010).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; AB496572; BAI77758.1; -; Genomic_DNA.
DR AlphaFoldDB; D3KTV3; -.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR011762; COA_CT_N.
DR InterPro; IPR041010; Znf-ACC.
DR PANTHER; PTHR42995; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR PANTHER; PTHR42995:SF5; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF17848; zf-ACC; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chloroplast {ECO:0000313|EMBL:BAI77758.1};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plastid {ECO:0000313|EMBL:BAI77758.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 47..263
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT NON_TER 263
FT /evidence="ECO:0000313|EMBL:BAI77758.1"
SQ SEQUENCE 263 AA; 29181 MW; 03CAD41567614CD0 CRC64;
MSVRNRFEDK RKLGGLIGAF LEKATKGYVS SEREKDRHIT IDTNKGLWTR CDNCGNMLYV
RFLKQNKSVC EECGYHPPMT STERIELLID RDTRIPMDED MTAQDVLSFS DEDSHQNRII
TSQKRTGLTD AVQTGIGYLN GTPLALGVMD FQFMGGSMGS VVGEKITRLI EYATDKSLPI
IIVCASGGAR MQEGTLSLMQ MAKISSVLQI HQVQRSLLYI SVLTYPTTGG VTASFGMQGD
IIIAESKAYI AFAGKRVIEQ TLR
//