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Database: UniProt
Entry: E1QFB5_DESB2
LinkDB: E1QFB5_DESB2
Original site: E1QFB5_DESB2 
ID   E1QFB5_DESB2            Unreviewed;       522 AA.
AC   E1QFB5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Carboxyl transferase {ECO:0000313|EMBL:ADK84251.1};
DE            EC=6.4.1.3 {ECO:0000313|EMBL:ADK84251.1};
GN   OrderedLocusNames=Deba_0881 {ECO:0000313|EMBL:ADK84251.1};
OS   Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS   / 2st14).
OC   Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK84251.1, ECO:0000313|Proteomes:UP000009047};
RN   [1] {ECO:0000313|EMBL:ADK84251.1, ECO:0000313|Proteomes:UP000009047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC   {ECO:0000313|Proteomes:UP000009047};
RX   PubMed=21304732; DOI=10.4056/sigs.1243258;
RA   Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA   Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA   Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT   "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL   Stand. Genomic Sci. 3:276-284(2010).
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DR   EMBL; CP002085; ADK84251.1; -; Genomic_DNA.
DR   RefSeq; WP_013257705.1; NC_014365.1.
DR   AlphaFoldDB; E1QFB5; -.
DR   STRING; 644282.Deba_0881; -.
DR   KEGG; dbr:Deba_0881; -.
DR   eggNOG; COG4799; Bacteria.
DR   HOGENOM; CLU_018822_6_2_7; -.
DR   Proteomes; UP000009047; Chromosome.
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:SF4; PROPIONYL-COA CARBOXYLASE; 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:ADK84251.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009047};
KW   Transferase {ECO:0000313|EMBL:ADK84251.1}.
FT   DOMAIN          9..265
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          269..504
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   522 AA;  56844 MW;  09ADC0342A994645 CRC64;
     MTNSEAPTTK SKLEELERRN QEALLGGGEE RIKAQHAKGK LTARERIDQL LDEGTFQEFD
     RFVVHRCHDF DMDKQKIPGD GVVTGFGKID GRPVFLFSQD FTVFGGSLSG PFGEKVCKIM
     DLAVKAGAPV IGLNDSGGAR IQEGVVSLAS YGEIFRRNVL SSGVVPQISA IMGPCAGGAV
     YSPAITDFIF MVDQNSYMHI TGPQVIKTVT GEDVTSETVG GAKVHNTKSG VAQFMAKDGK
     ECLAQVRQLL SYLPSNWEQK PPYLATGDDP RRTCPELDQI IPDNPKSPYN MKQLIKTVVD
     QGTFFEAAKH WAKNMITAFA RMGGNAVGIV ANNPMHMAGC LDIDASRKCA RFVRFCDAFN
     IPVVTFVDVP GFLPGVQQEY GGIITHGSKV IYAYCEATVP LITIITRKAY GGAYDVMGSK
     HHGADVNFAF PTAEIAVMGP EGAVNIVFRK QLNDATDKAA AYAELVADYR KNIASPYRAA
     ELGYIDEIIM PHSTRAKVIQ ALEALKGKRT FRPVRRHGNV PL
//
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