ID C5T3M3_ACIDE Unreviewed; 539 AA.
AC C5T3M3;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Carboxyl transferase {ECO:0000313|EMBL:EER60929.1};
GN ORFNames=AcdelDRAFT_1506 {ECO:0000313|EMBL:EER60929.1};
OS Acidovorax delafieldii 2AN.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER60929.1, ECO:0000313|Proteomes:UP000003856};
RN [1] {ECO:0000313|EMBL:EER60929.1, ECO:0000313|Proteomes:UP000003856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2AN {ECO:0000313|EMBL:EER60929.1,
RC ECO:0000313|Proteomes:UP000003856};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA Picardal F., Roden E., Emerson D.;
RT "The draft genome of Acidovorax delafieldii 2AN.";
RL Submitted (MAY-2009) 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:EER60929.1}.
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DR EMBL; ACQT01000033; EER60929.1; -; Genomic_DNA.
DR RefSeq; WP_005795075.1; NZ_ACQT01000033.1.
DR AlphaFoldDB; C5T3M3; -.
DR PATRIC; fig|573060.9.peg.3660; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000003856; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR PANTHER; PTHR43842:SF4; PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000003856};
KW Transferase {ECO:0000313|EMBL:EER60929.1}.
FT DOMAIN 291..531
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 539 AA; 58443 MW; 8BA5A5056C55581A CRC64;
MTPSQQTPHI PPPEADPSAP LWQPELVELS QRHAYAEAMG GPYAVARHRA NGKLTIRERI
RTLADEGSFQ EIGKLTGQGS YADGRLTGLT PAPYVMGLAQ IDGRDVAIGG EDFTIRGGAS
WSGDRKKGGQ GGFVEDLALH YRMPLVNLVD GAGGSVGAQR KRGHTVFPGV HGFETSVDLL
GTVPVVSAVL GSAAGGPAGR AILSHWSVMT PGSGHIFAAG PPVVERSLGQ KITKEELGGA
RVAVEQAGLV DNVAPDEHAC FAMVRRYLSY MPRNVWELPP AIDATDPPWR REERLASIVP
RDRRRAYDMR QLLTLVADQE SLFEIQPTYG RALITSLGRL NGKVAGFIAN NPRHYGGAMD
VQAARKQTHF IELCDTFHIP LVFLVDVPGF MVGRDAEAAG TLREGMRSVY TALQASVPMI
TVVIRKCYGM AGMATTDKRG IGLKLAWPSA EWGSLPLEGG VAAAFRREIA DAPHPALRER
EIEAELRALS SPFRTAEAFG VEDIIDPRDT RRYLCRFIDA VQPRLRTELG PKARYGVRP
//
