ID   A4TFI9_MYCGI            Unreviewed;       539 AA.
AC   A4TFI9;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Carboxyl transferase {ECO:0000313|EMBL:ABP47081.1};
GN   OrderedLocusNames=Mflv_4613 {ECO:0000313|EMBL:ABP47081.1};
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP47081.1};
RN   [1] {ECO:0000313|EMBL:ABP47081.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP47081.1};
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABP47081.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP47081.1};
RX   PubMed=23469141;
RA   Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT   "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT   Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT   during Pyrene Degradation.";
RL   PLoS ONE 8:E58066-E58066(2013).
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC       {ECO:0000256|ARBA:ARBA00006102}.
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DR   EMBL; CP000656; ABP47081.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4TFI9; -.
DR   STRING; 350054.Mflv_4613; -.
DR   KEGG; mgi:Mflv_4613; -.
DR   eggNOG; COG4799; Bacteria.
DR   HOGENOM; CLU_018822_0_1_11; -.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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   InterPro; IPR045190; MCCB/AccD1-like.
DR   PANTHER; PTHR22855; ACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED; 1.
DR   PANTHER; PTHR22855:SF46; METHYLCROTONOYL-COA CARBOXYLASE; 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   3: Inferred from homology;
KW   Transferase {ECO:0000313|EMBL:ABP47081.1}.
FT   DOMAIN          26..280
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          283..530
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   539 AA;  57815 MW;  65776401A7E4BC1B CRC64;
     MSPGGKLIDV LPDRVDTRAP VYLENREGLI AQLHALAEQL ALANGGGGEK YVARHRSRGK
     MLARERVELL LDPDTAFLEL CPFAAWGTKF PVGGSVVVGI GIVEGVESMI IAHDPTVRGG
     ASNPYTFRKV FRGMAVAREN RLPIINVVES GGADLPTQAE IFVPGGQLFN DLTQHSALGL
     PTLALVFGNS TAGGAYIPGM CDYVVMVRNR SKVFLGGPPL VKMATGEVSD DESLGGADMH
     ARTSGLADYM AEDEQDAIRI GRRIMARLNW RKLGPGPTQP PTPPLRDPDQ LLGIASVDPK
     VPFDPRDVIA RIVDGSTFDE FKPLYGTSLV TGWASIHGYP VGILANARGI LFSEEAEKAA
     QFIQLANQID TPLVFLQNTT GYMVGAEYEQ GGIIKDGAKM INAVSNSAVP HLTIVMGASY
     GAGNYGMCGR SYSPRFLFTW PNSRSAVMGP AQLAGVLSIV ARESAADRGL PFDEEADAQM
     RAAVEGQIER ESLALANSGR LYDDGIIDPR DTRTVLGFCL SVVHNSEIRG QRGYGVFRM
//