ID C1CZX8_DEIDV Unreviewed; 520 AA.
AC C1CZX8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Putative propionyl-CoA carboxylase beta chain (PCCase) (Propanoyl-CoA:carbon dioxide ligase) {ECO:0000313|EMBL:ACO45230.1};
GN OrderedLocusNames=Deide_04040 {ECO:0000313|EMBL:ACO45230.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO45230.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO45230.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001114; ACO45230.1; -; Genomic_DNA.
DR RefSeq; WP_012692353.1; NC_012526.1.
DR AlphaFoldDB; C1CZX8; -.
DR STRING; 546414.Deide_04040; -.
DR PaxDb; 546414-Deide_04040; -.
DR KEGG; ddr:Deide_04040; -.
DR eggNOG; COG4799; Bacteria.
DR HOGENOM; CLU_018822_6_2_0; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000002208; Chromosome.
DR GO; GO:0016874; F:ligase 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 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 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:ACO45230.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208}.
FT DOMAIN 8..263
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 267..513
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 16..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 56698 MW; D6D06978E6BAFD77 CRC64;
MTQPGVELQE LIAAMEQRRH KVEQGGGPER QKKQKEGGKL TARERIEHLL DPGSFLEMST
FVEHGRNRLM EGVDAPGEGV VTGRGTIDGR QVFVFSQDFT VLGGSLGKMN ASKVTKIMDL
AAKTGCPVIG LNDSAGARIQ EGVDSLSGYG EIFYRNAIYS GSVPQISAIL GPCAGGAVYS
PALTDFILMS RGTSYMFITG PEVIKSVTRE EVTFDTLGGA DVHTRKSGVA HLAYDGDEAV
LDGVRDLLGY LPQNAREHPP VKPTQDPPNR SNERLLELVT PDQRKPYAMH DVIRELVDEG
TFLEIQPDWA KNMLVGFARL GGQSVGIVAN NPKSMAGTLN IDASDKAARF IRTCDCYNIP
ILTLVDVTGF LPGTQQEYGG IIRHGAKMLY AYAEASVPKV TLITRKSYGG AYLAMNSRDM
GADVVYAWPI AAVAVMGAEG AANIVYRRDI NSSDNPEATR AQKIAEYKEA FDNPYVAAAK
GYIDDVIPME ETRARLIQTF EMLRNKEETR PYKKHGNMPL
//
