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ACCD_CHLSC
ID   ACCD_CHLSC              Reviewed;         502 AA.
AC   A6MMD1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01395};
DE            Short=ACCase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE            Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
DE            EC=2.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01395};
GN   Name=accD {ECO:0000255|HAMAP-Rule:MF_01395};
OS   Chloranthus spicatus (Chulantree) (Nigrina spicata).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Chloranthales; Chloranthaceae; Chloranthus.
OX   NCBI_TaxID=13006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17644003; DOI=10.1016/j.ympev.2007.06.004;
RA   Hansen D.R., Dastidar S.G., Cai Z., Penaflor C., Kuehl J.V., Boore J.L.,
RA   Jansen R.K.;
RT   "Phylogenetic and evolutionary implications of complete chloroplast genome
RT   sequences of four early-diverging angiosperms: Buxus (Buxaceae),
RT   Chloranthus (Chloranthaceae), Dioscorea (Dioscoreaceae), and Illicium
RT   (Schisandraceae).";
RL   Mol. Phylogenet. Evol. 45:547-563(2007).
CC   -!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex.
CC       Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its
CC       carrier protein (BCCP) and then the CO(2) group is transferred by the
CC       transcarboxylase to acetyl-CoA to form malonyl-CoA. {ECO:0000255|HAMAP-
CC       Rule:MF_01395}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC         CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC         Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01395};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01395};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01395};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01395}.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000255|HAMAP-
CC       Rule:MF_01395}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01395}.
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DR   EMBL; EF380352; ABQ43269.1; -; Genomic_DNA.
DR   RefSeq; YP_001294107.1; NC_009598.1.
DR   AlphaFoldDB; A6MMD1; -.
DR   SMR; A6MMD1; -.
DR   GeneID; 5236453; -.
DR   UniPathway; UPA00655; UER00711.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011762; COA_CT_N.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR00515; accD; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Metal-binding; Nucleotide-binding;
KW   Plastid; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..502
FT                   /note="Acetyl-coenzyme A carboxylase carboxyl transferase
FT                   subunit beta, chloroplastic"
FT                   /id="PRO_0000359129"
FT   DOMAIN          226..497
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   ZN_FING         230..252
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   REGION          191..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         230
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   BINDING         233
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
FT   BINDING         252
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01395"
SQ   SEQUENCE   502 AA;  56709 MW;  42626FF86B37D2CF CRC64;
     MEKWWFNSML SNEELEHRWG LSKSMESLGP IGNTRGSEDP IINDTDKNIH SYSWSDSGSY
     SCSNVDHFFG VSDIWSFISD ETFLVRDSNG KGYSVYFDIE NRIFEIDNDS SFLSELESSF
     SSYLSNGSKN DNRYYDSYMY DTKYSWNNHM NSCIDSYLRS EISIDSYIST GSDNFSDSYI
     YSYIFSEKVS GSDSESSSIR TSGNDSNFNV RERDNDFDRN QKYGRLWVQC ENCYELNYRS
     FFRSKMNICE QCGYHLKMNS LDRIELSIDS GTWNPMDDDM VSMDPIEFHS MEEPYRDRID
     SYQRNTGLTE AVQTGIGQLN GIPIAIGVMD FQFMGGSMGS VVGEKITRLI EYATNESIPV
     IMVCASGGAR MQEGSLSLMQ MAKISSASYN YQLNKKLFYV SILTSPTTGG VTASFGMLGD
     IIIAEPNAYI AFAGKRVIEQ TLNKTVPDGS QVAEYSFHKG LFDPIVPRNP LKGVLSELFQ
     LHGFFPLNQN SSGARGSVIC SE
 
 
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