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Database: UniProt
Entry: A4J3E6_DESRM
LinkDB: A4J3E6_DESRM
Original site: A4J3E6_DESRM 
ID   A4J3E6_DESRM            Unreviewed;       634 AA.
AC   A4J3E6;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562};
GN   OrderedLocusNames=Dred_1064 {ECO:0000313|EMBL:ABO49599.1};
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO49599.1, ECO:0000313|Proteomes:UP000001556};
RN   [1] {ECO:0000313|EMBL:ABO49599.1, ECO:0000313|Proteomes:UP000001556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MI-1 {ECO:0000313|EMBL:ABO49599.1,
RC   ECO:0000313|Proteomes:UP000001556};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
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DR   EMBL; CP000612; ABO49599.1; -; Genomic_DNA.
DR   RefSeq; WP_011877425.1; NC_009253.1.
DR   AlphaFoldDB; A4J3E6; -.
DR   STRING; 349161.Dred_1064; -.
DR   KEGG; drm:Dred_1064; -.
DR   eggNOG; COG0511; Bacteria.
DR   eggNOG; COG5016; Bacteria.
DR   HOGENOM; CLU_000395_4_3_9; -.
DR   OrthoDB; 9807469at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001556; 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:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR001249; AcCoA_biotinCC.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR00531; BCCP; 1.
DR   PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   PRINTS; PR01071; ACOABIOTINCC.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001556}.
FT   DOMAIN          5..265
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          556..632
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          442..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          516..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   634 AA;  70115 MW;  A60525601AFC828E CRC64;
     MSHHLKITDT TLRDAHQSLW ATRMATEDML PILEKLDQMG YHSLEVWGGA TFDVCLRFLN
     EDPWERLRLI RKYVKNTPLQ MLLRGQSLLG YMHYPDDVLE AFIHKTVENG MDIIRIFDAL
     NDIRNMEKAI QATKAAGAHA QATVVYTVSP VHTTEHYLET ALRLEEMGAD SICIKDMAGL
     LAPFKSYELV KLFKAHLQVP VQLHCHYIGG MAVGAYLKAA EAGVDVVDTA SVPMAFGASQ
     PPVETVVRAL KGTPYDTGLS MKALFEVAQY FEDIRKVLGQ QRGVTRISDM RVFEHQVPGG
     MISNLVSQLE EQKALHRLDE VLEEIPRVRE ELGFPPLVTP TSQIVGTQAV LNVLTGQRYK
     LIPGEVKLYV EGYYGQPPAT IDPSVSRKVL GDKEAISCRP ADLLEPKLDK LRDEIKDLAI
     SQEDILSYAM FPQVARKFFE ARKRGETGPQ RKEASIKPGA PADFSGTKST KEAKNVNLSE
     LKELIKVLDQ TDITEIDLES DGVKVSIRKG GKVSATVTPA APQKTAETPV TEAPKTGEAS
     VAPEVPVVST QPTEDLIPVT APMVGTFYRA PSPDADPFVN VGDIVEKGQT LCIVEAMKLM
     NEIEAEQAGE IVQIMVENGQ PIEYGQNLFM IRKK
//
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