ID A0A0G3GN62_9CORY Unreviewed; 501 AA.
AC A0A0G3GN62;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acetyl-CoA carboxylase beta subunit {ECO:0000313|EMBL:AKK02616.1};
DE EC=6.4.1.2 {ECO:0000313|EMBL:AKK02616.1};
GN Name=accD3 {ECO:0000313|EMBL:AKK02616.1};
GN ORFNames=CEPID_03710 {ECO:0000313|EMBL:AKK02616.1};
OS Corynebacterium epidermidicanis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK02616.1, ECO:0000313|Proteomes:UP000035368};
RN [1] {ECO:0000313|EMBL:AKK02616.1, ECO:0000313|Proteomes:UP000035368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK02616.1,
RC ECO:0000313|Proteomes:UP000035368};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium epidermidicanis DSM 45586,
RT isolated from the skin of a dog suffering from pruritus.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC {ECO:0000256|ARBA:ARBA00006102}.
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DR EMBL; CP011541; AKK02616.1; -; Genomic_DNA.
DR RefSeq; WP_047239789.1; NZ_CP011541.1.
DR AlphaFoldDB; A0A0G3GN62; -.
DR STRING; 1050174.CEPID_03710; -.
DR KEGG; cei:CEPID_03710; -.
DR PATRIC; fig|1050174.4.peg.753; -.
DR OrthoDB; 9772975at2; -.
DR Proteomes; UP000035368; Chromosome.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; 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 PRINTS; PR01070; ACCCTRFRASEB.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:AKK02616.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035368};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..239
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 223..477
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 501 AA; 53449 MW; 725EBBC4FED06840 CRC64;
MSSTTRTSAN DLITTVLDPG SFISWDTSPE YGDISDDYRE ALARAREKSG VDESVITGEG
TVAGRRVATI VSEFSFLGGS IGAATARRII AGIHRATAER LPLLISPSSG GTRMQEGTPA
FALMVSITTA VYRHKDAHLP FLVYLRNPTT GGVMASWGSA GHFTFAEPGA LLGFLGPRVV
ELTTGTPIPD GVQSGENLAH VGVIDGVLSP KLLRDAVRKI EDVLLSTHSD LEPTRPETAE
VAAGNVWESI LKTRQADRPG VRDIVAKLSP KLIELSGSGD GRRSAAMTVA LAQIAGRPVV
LIGQNRHQQP PLGEAELGPE ALRCARRGIA LAHELQLPLV SIIDTPGAEL SQHAEEHGLA
GSIARTLGEL VYLDVPTISV ILGQGCGGGA LAMLPADRVL AAEHAWLSPL PPEGASAIIY
RDIDHAPQMM EEQDVSAFAL HRAGIVDSII PEQPDAAEEP EAFIDRVLST ISHELWVLEN
SPERVGREQR FKHYEKLATR Q
//
