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Database: UniProt
Entry: I9AVR8_9FIRM
LinkDB: I9AVR8_9FIRM
Original site: I9AVR8_9FIRM 
ID   I9AVR8_9FIRM            Unreviewed;       509 AA.
AC   I9AVR8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Carboxyl transferase {ECO:0000313|EMBL:EIW17007.1};
GN   ORFNames=FB4_4363 {ECO:0000313|EMBL:EIW17007.1};
OS   Pelosinus fermentans B4.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW17007.1, ECO:0000313|Proteomes:UP000004324};
RN   [1] {ECO:0000313|EMBL:EIW17007.1, ECO:0000313|Proteomes:UP000004324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:EIW17007.1,
RC   ECO:0000313|Proteomes:UP000004324};
RX   PubMed=22933770; DOI=10.1128/JB.01174-12;
RA   Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA   Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA   Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT   "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT   Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL   J. Bacteriol. 194:5147-5148(2012).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIW17007.1}.
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DR   EMBL; AKVJ01000031; EIW17007.1; -; Genomic_DNA.
DR   RefSeq; WP_007936178.1; NZ_AKVJ01000031.1.
DR   AlphaFoldDB; I9AVR8; -.
DR   PATRIC; fig|1149862.3.peg.3332; -.
DR   OrthoDB; 9803706at2; -.
DR   Proteomes; UP000004324; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   PANTHER; PTHR43842:SF2; BIOTIN-DEPENDENT ACETYL-_PROPIONYL-COENZYME A CARBOXYLASE BETA5 SUBUNIT; 1.
DR   PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000313|EMBL:EIW17007.1}.
FT   DOMAIN          4..260
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          264..491
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   509 AA;  55138 MW;  7919EB6C2B3B8B88 CRC64;
     MATVQEKIED LKARQEKIKL GGGQKRIDKQ HATGKLTARE RVEKLLDPNT FVELDQFVTH
     RCVNFDMASV DAPAEGVVTG YGTIEGRLVY VFAQDFTVVG GSLGEMHAAK IVKVQQLALK
     MGAPIIGIND SGGARIQEAV DALAGYGKIF YNNTLASGVI PQISVIMGPC AGGAVYSPAL
     TDFIYMVKNT SQMFITGPQV IKSVTAEEVT AEALGGAMTH NTTSGVAHFV AENDEDCLEQ
     IRCLMSFLPG NNLEGSPVVL NTDDVNRMED SLNTLLPDNP NQPYNMKDII SAIVDNGDFY
     EVQPYFARNI LTCFARFDGQ TVGIIANQPS VMAGCLDVDA SDKSARFIRF CDAFNIPLVN
     LVDVPGFLPG VSQEYGGIIR HGAKMLYAYS EATVPKVTVI TRKAYGGSYL AMCSQDLGAD
     QVMAWPTSEI AVMGPAGAAN IIFRGDPDVK AKTEEYIAEF ATPYKAAERG FVDQVIEPKE
     TRPRIITALS MLASKREQRP QKKHGNIPL
//
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