ID   A1UL75_MYCSK            Unreviewed;       530 AA.
AC   A1UL75;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Propionyl-CoA carboxylase {ECO:0000313|EMBL:ABL93583.1};
DE            EC=6.4.1.3 {ECO:0000313|EMBL:ABL93583.1};
GN   OrderedLocusNames=Mkms_4392 {ECO:0000313|EMBL:ABL93583.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL93583.1};
RN   [1] {ECO:0000313|EMBL:ABL93583.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL93583.1};
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   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC       {ECO:0000256|ARBA:ARBA00006102}.
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; CP000518; ABL93583.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UL75; -.
DR   STRING; 189918.Mkms_4392; -.
DR   KEGG; mkm:Mkms_4392; -.
DR   HOGENOM; CLU_018822_0_1_11; -.
DR   OrthoDB; 9803706at2; -.
DR   GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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   Ligase {ECO:0000313|EMBL:ABL93583.1}.
FT   DOMAIN          21..272
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          274..521
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   530 AA;  56188 MW;  10D03E17B5696813 CRC64;
     MALKSTLDPS SPGYAAAADA MAAKLAELET EHAKALAGGG AKYVERHHAR GKLTARERIE
     LLLDPDSPFL ELSPLAAWGS EFTVGASVVT GIGAVSGVEC LLVANDPTVK GGTSNPWTLR
     KILRANQIAL QNPLPVISLV ESGGADLPTQ KEVFIPGGQM FRDLTRLSAA GIPTIALVFG
     NSTAGGAYVP GMSDHVVMIK ERSKVFLAGP PLVKMATGEE SDDESLGGAE MHARTSGLAD
     YFALDELDAL RIGRRIVGRL NWRKQGPAPA PVTEPLFDSE ELLGIVPADL RIPFDPRDVV
     ARIVDGSEFD EFKALYGSSL VTGWARLHGY PIGILANARG VLFSEESQKA TQFIQLANRS
     NTPLLFLHNT TGYMVGRQYE EGGMIKHGSM MINAVSNSTV PHLSLLIGAS YGAGHYGMCG
     RAYDPRFLFA WPSAKAAVMG GTQLAGVISI VGRAAAEARG QVVDEDADAA LRAAIEAQIE
     AESLPMFLSG RLYDDGVIDP RDTRTVLGMC LSAIANGPIE GTSNFGVFRM
//