ID F6B9R0_DESCC Unreviewed; 635 AA.
AC F6B9R0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562};
GN OrderedLocusNames=Desca_2117 {ECO:0000313|EMBL:AEF94956.1};
OS Desulfotomaculum nigrificans (strain DSM 14880 / VKM B-2319 / CO-1-SRB)
OS (Desulfotomaculum carboxydivorans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=868595 {ECO:0000313|EMBL:AEF94956.1, ECO:0000313|Proteomes:UP000009226};
RN [1] {ECO:0000313|Proteomes:UP000009226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14880 / VKM B-2319 / CO-1-SRB
RC {ECO:0000313|Proteomes:UP000009226};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stams A., Plugge C., Muyzer G.,
RA Kuever J., Parshina S., Ivanova A., Nazina T., Woyke T.;
RT "Complete sequence of Desulfotomaculum carboxydivorans CO-1-SRB.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
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DR EMBL; CP002736; AEF94956.1; -; Genomic_DNA.
DR RefSeq; WP_013810554.1; NC_015565.1.
DR AlphaFoldDB; F6B9R0; -.
DR STRING; 868595.Desca_2117; -.
DR KEGG; dca:Desca_2117; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR HOGENOM; CLU_000395_4_2_9; -.
DR OMA; GYHALEM; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000009226; 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 Ligase {ECO:0000313|EMBL:AEF94956.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009226}.
FT DOMAIN 5..265
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 557..633
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 442..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 69642 MW; FCEDB9F8D4D8534F CRC64;
MTHRLKITDT SLRDGHQSLW ATRMATEDML PILEKLDQMG FHSLEVWGGA TFDVCLRFLN
EDPWERLRLI KKHVKNTPLQ MLLRGQSLLG YMHYPDDILE AFIHKTVENG MDIIRIFDAL
NDIRNMERAI QVTKQAGAHA QATVVYTISP VHTTEHYLET ALRLEELGAD SICIKDMAGL
LAPFKAYELV KLFKSHLSVP VQLHCHYIGG MAVGAYLKAA EAGVDVVDTA SVPMAFGASQ
PPVETVVRAL KGTPYDTGLS IKALFEIAQY FEDLRKELGQ QRGVTRINDM RVFEHQVPGG
MISNLVSQLE EQKALHRLDE VLEEIPRVRE ELGYPPLVTP TSQIVGTQAV LNVLTGQRYK
LIPGEVKLYV QGYYGQPPAS IDPAISRKVL GDKEMITCRP ADLLEPKLDK LREEIKDLAV
SEEDVLSYAM FPQVARKFFE ARKRGETGPH RKAASVKPGS PADTNAAKST KEANNVNLNE
LKELIKVLDQ TDITEIELES DGVKVSIRKG GKVSAAPVAP APTATTPEAP AVTKAAEATV
APAPAAAPAP AVPAADLTPV TAPMVGTFYR APAPDADPFV KVGDTVQAGQ TLCIIEAMKL
MNEIEAEVSG EVVEILVENG QPVEYGQTLF LIKKK
//