ID A0A087BMC0_9BIFI Unreviewed; 511 AA.
AC A0A087BMC0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Carboxyl transferase domain-containing protein {ECO:0000313|EMBL:KFI72170.1};
DE EC=6.4.1.3 {ECO:0000313|EMBL:KFI72170.1};
GN ORFNames=BMIN_0059 {ECO:0000313|EMBL:KFI72170.1};
OS Bifidobacterium minimum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1693 {ECO:0000313|EMBL:KFI72170.1, ECO:0000313|Proteomes:UP000029014};
RN [1] {ECO:0000313|EMBL:KFI72170.1, ECO:0000313|Proteomes:UP000029014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11592 {ECO:0000313|EMBL:KFI72170.1,
RC ECO:0000313|Proteomes:UP000029014};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KFI72170.1}.
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DR EMBL; JGZD01000009; KFI72170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087BMC0; -.
DR STRING; 1693.BMIN_0059; -.
DR eggNOG; COG4799; Bacteria.
DR Proteomes; UP000029014; 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:0004658; F:propionyl-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; 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 Ligase {ECO:0000313|EMBL:KFI72170.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029014};
KW Transferase {ECO:0000313|EMBL:KFI72170.1}.
FT DOMAIN 26..275
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 280..511
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 54377 MW; 7876DE16CFF01493 CRC64;
MSISMRERTD GAVGRAGAPS PAEADRQPLR PAISRAADLA RAGENRACAK QHAKGKKTAR
ERLDLLFDPG SFRETGRFIG ADINNDRSGC AVVTGMGQVR GRTVAAYAQD FSIRGGTLGA
VEGDKILRLM DEAMRIGAPI VALLDSGGAR IQEGVAALSR YGGIFRATCR ASGTVPQISI
ILGPCAGGAV YCPALTDLII MTRENSHMFV TGPDVVREAT GETIGMDELG GGLLHGTVSG
VAHYLAQDET DAIDYARVVL SYLPSNCMEQ APRYDYVATR ADRRTADALS SIVPERDREP
YDMREVIGLI VDYGEFVQVH EMYAGSALTG FACIDGRSVG IVANQPSVMG GVLDVESSEK
IARFVRLCDA FNLPVVTLVD TPGYRPGSDQ ERAGIIRRGA KVIYAYAEAQ VPLVTVVLRK
AFGGAYIVMG SRSIGADEVF AWPTSRIAVL GAKGAVDIIH RRDLITAREG GGGRRGSSPD
VGGRLREPCG QREPGSGDGT DRRDDRSRAD P
//
