ID F6DUA8_DESRL Unreviewed; 632 AA.
AC F6DUA8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562};
GN OrderedLocusNames=Desru_3082 {ECO:0000313|EMBL:AEG61293.1};
OS Desulforamulus ruminis (strain ATCC 23193 / DSM 2154 / NCIMB 8452 / DL)
OS (Desulfotomaculum ruminis).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=696281 {ECO:0000313|EMBL:AEG61293.1, ECO:0000313|Proteomes:UP000009234};
RN [1] {ECO:0000313|Proteomes:UP000009234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC {ECO:0000313|Proteomes:UP000009234};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Mikhailova N., Pagani I., Stams A.J.M., Plugge C.M., Muyzer G.,
RA Kuever J., Parshina S.N., Ivanova A.E., Nazina T.N., Brambilla E.,
RA Spring S., Klenk H.-P., Woyke T.;
RT "Complete sequence of Desulfotomaculum ruminis DSM 2154.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG61293.1, ECO:0000313|Proteomes:UP000009234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23193 / DSM 2154 / NCIB 8452 / DL
RC {ECO:0000313|Proteomes:UP000009234};
RX PubMed=23408247; DOI=10.4056/sigs.3226659;
RA Spring S., Visser M., Lu M., Copeland A., Lapidus A., Lucas S., Cheng J.F.,
RA Han C., Tapia R., Goodwin L.A., Pitluck S., Ivanova N., Land M., Hauser L.,
RA Larimer F., Rohde M., Goker M., Detter J.C., Kyrpides N.C., Woyke T.,
RA Schaap P.J., Plugge C.M., Muyzer G., Kuever J., Pereira I.A.,
RA Parshina S.N., Bernier-Latmani R., Stams A.J., Klenk H.P.;
RT "Complete genome sequence of the sulfate-reducing firmicute
RT Desulfotomaculum ruminis type strain (DL(T)).";
RL Stand. Genomic Sci. 7:304-319(2012).
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
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; CP002780; AEG61293.1; -; Genomic_DNA.
DR RefSeq; WP_013843045.1; NC_015589.1.
DR AlphaFoldDB; F6DUA8; -.
DR STRING; 696281.Desru_3082; -.
DR KEGG; dru:Desru_3082; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR HOGENOM; CLU_000395_4_2_9; -.
DR OrthoDB; 9807469at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000009234; 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:UP000009234}.
FT DOMAIN 5..265
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 554..630
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 632 AA; 69737 MW; D9B80BFD028D63AE CRC64;
MTHRLRITDT SLRDGHQSLW ATRMATEDML PIAEKLDQMG YHSLEVWGGA TFDVCLRFLN
EDPWERLRLI KKQVKNTPLQ MLLRGQSLVG YMHYPDDILE AFIHKVVENG MDIIRIFDAL
NDIRNMEKSI QITKKAGAHA QATVVYTVSP VHTTEHYLET ALRLEEMGAD SICIKDMAGL
LAPFKAYELV KLFKAHLNIP IHLHCHYIGG MAVGAYLKAA EAGVDVVDTA SVPMAFGASQ
PPVETVVRAL KGTPYDTGLS LRSLFEIAQY FEELRKGLGQ QRGVTRINDM RVFEHQVPGG
MISNLVSQLE EQKALHRLDE VLEEIPRVRE ELGYPPLVTP TSQIVGTQAV LNVLTGQRYK
LIPGEVKLYV QGYYGRPPAT IDPSVSRNVL GGKEMITCRP ADLLEPKLDK LREEIKDLAI
SQEDVLSYAL FPQVARKFFE ARKRGETGPH RKSVSIKPGA PADVNAIKRT KEANNVNLNE
LKELIKVLDQ TDITEIDLES DGVKVSIRKG GKVSSVRTGP AAEPTETPAA VKTVEEPVAP
PAAPAAAPAV AENLIPVTAP MVGTFYRASA PDADPFVNVG DVVEPGRTLC IIEAMKLMNE
IEAEAAGEIV DILVENGQPV EFGQTLFLIK KK
//
