ID Q32XZ2_9MONI Unreviewed; 255 AA.
AC Q32XZ2;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Acetyl-CoA carboxylase beta subunit {ECO:0000313|EMBL:AAW50333.1};
DE Flags: Fragment;
GN Name=accD {ECO:0000313|EMBL:AAW50333.1};
OS Hymenophyllum flabellatum.
OG Plastid; Chloroplast {ECO:0000313|EMBL:AAW50333.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Hymenophyllales; Hymenophyllaceae;
OC Hymenophylloideae; Hymenophyllum.
OX NCBI_TaxID=191647 {ECO:0000313|EMBL:AAW50333.1};
RN [1] {ECO:0000313|EMBL:AAW50333.1}
RP NUCLEOTIDE SEQUENCE.
RX DOI=10.1600/036364406777585775;
RA Hennequin S., Ebihara A., Ito M., Iwatsuki K., Dubuisson J.Y.;
RT "New insights into the phylogeny of the genus Hymenophyllum s.l.
RT (Hymenophyllaceae): revealing the polyphyly of Mecodium.";
RL Syst. Bot. 31:271-284(2006).
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; AY775442; AAW50333.1; -; Genomic_DNA.
DR AlphaFoldDB; Q32XZ2; -.
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:AAW50333.1};
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:AAW50333.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 47..255
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT NON_TER 255
FT /evidence="ECO:0000313|EMBL:AAW50333.1"
SQ SEQUENCE 255 AA; 28101 MW; FF27EF36E04966C4 CRC64;
MSVRNRFEDK RKLGGLIGAF LEKATKGYVS SEREKDRPIT IDTNKGLWTR CDNCGNMLYV
RFLKQNKSVC EECGYHPPMT STERIELLID RDTRIPMDED MTAQDVLSFS DEDSHQNRII
TSQKRTGLTD AVQTGIGYLN GTPLALGVMD FQFMGGSMGS VVGEKITRLI EYATDKSLPI
IIVCASGGAR MQEGTLSLMQ MAKISSVLQI HQVQKSLLYI SVLTYPTTGG VTASFGMLGD
IIIAESKAYI AFAGK
//
