ID   A5D314_PELTS            Unreviewed;       659 AA.
AC   A5D314;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00017562};
GN   OrderedLocusNames=PTH_1174 {ECO:0000313|EMBL:BAF59355.1};
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF59355.1, ECO:0000313|Proteomes:UP000006556};
RN   [1] {ECO:0000313|Proteomes:UP000006556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT   evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
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DR   EMBL; AP009389; BAF59355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5D314; -.
DR   STRING; 370438.PTH_1174; -.
DR   KEGG; pth:PTH_1174; -.
DR   eggNOG; COG0511; Bacteria.
DR   eggNOG; COG5016; Bacteria.
DR   HOGENOM; CLU_000395_4_2_9; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000006556; 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:UP000006556}.
FT   DOMAIN          4..264
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          581..657
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          468..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..572
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   659 AA;  72520 MW;  CBD2236AA2492C37 CRC64;
     MRRVKITDTT LRDAHQSLWA TRMTTADMLP VAEKLDKIGY HSIEVWGGTT FDVCLRYLNE
     DPWERLRQLK KIIRHTPLQM LIRGQSLVGY KHYPDDVVES FVTKAVENGI NIIRVFDALN
     DIRNLETAMR AGKAAGAHVQ AAMVYTVSPV HTGQHYLELA LRLAEMGADS ICLKDMAGLL
     DPYRAYELVK LLKENLDLPL QCHCHYIGGL AFGTYLKAVE AGADVIDTAT LPLAFGASLP
     PVETVVRALQ GSPYDTGLNI RELFEIAKYF EELRKENGFK RGVTRINDMR VFDHQVPGGT
     ISNLVTQLEE QKSLYRLGEV MEEIPRVREE LGYPPLVTPA SQIVGTQAVL NVLTGERYKL
     VPGEVRDYIR GSYGTPPAPI NREIARKVLG DREPVTCRPA DLLEPVMGKI RNEVGELALS
     EEDVISYALF PQVARRFLEL RRSGGLGRPE PQNEKNVNMR VNNAARAGAG VPAGTAKESS
     AKKVAQVPPA EAGSAGTVEK EAGELNLHDI RELIRLIDET SITEVSLENA GLRVAIKKGG
     TCGVKAAGPE PEQKVQTVPR DTTEEEPAKT ARPADNLKAG AVPVVSPMVG TFYRSPAPDA
     PPFVKVGDRV QKGQTLCIIE AMKLMNEIEA EVSGEIVEIL VENGQPVEYG QTLFLIKEK
//