ID   A0A1H9PGU2_9PSEU        Unreviewed;       537 AA.
AC   A0A1H9PGU2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=3-methylcrotonyl-CoA carboxylase beta subunit {ECO:0000313|EMBL:SER47442.1};
GN   ORFNames=SAMN04487818_103451 {ECO:0000313|EMBL:SER47442.1};
OS   Actinokineospora terrae.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=155974 {ECO:0000313|EMBL:SER47442.1, ECO:0000313|Proteomes:UP000199051};
RN   [1] {ECO:0000313|EMBL:SER47442.1, ECO:0000313|Proteomes:UP000199051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44260 {ECO:0000313|EMBL:SER47442.1,
RC   ECO:0000313|Proteomes:UP000199051};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOGI01000003; SER47442.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9PGU2; -.
DR   STRING; 155974.SAMN04487818_103451; -.
DR   Proteomes; UP000199051; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
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:SF13; METHYLCROTONOYL-COA CARBOXYLASE BETA CHAIN, MITOCHONDRIAL; 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   Reference proteome {ECO:0000313|Proteomes:UP000199051}.
FT   DOMAIN          24..280
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          280..529
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   537 AA;  57523 MW;  1F071B5E442E6D7C CRC64;
     MDAPRLRSAV DPADEAFQRN VTSHDELVHD LRERLDQAAL GGPEKARARH VGRGKLLPRD
     RVDSLLDPGS PFLELSPLAA TGLYGDDAPA AGVITGVGRV SGREVVVVVN DATVKGGTYY
     PMTVKKHLRA QEVALQNNLP CVYLVDSGGA FLPKQDDVFP DRDHFGRIFF NQATMSAKGI
     PQIAAVLGSC TAGGAYVPAM SDEAVIVRDQ GTIFLGGPPL VKAATGEVVT AEELGGGDVH
     SRVSGVTDHL ADDDAHALRI VRSIVSTLGP RAPRPWEVAP VEEPAVDPST LYGVVPTDSR
     TPYDVREVIA RVVDGSRFRE FKKEYGSTLV TGFARIHGHP VGIVANNGVL FAESAMKGAH
     FIELCDQRSI PLLYLQNITG FMVGRDYEAG GIAKHGAKMV TATACARVPK FTVVIGGSFG
     AGNYSMCGRA YSPRFLWMWP NARISVMGGE QAASVLSTVR RDQIEGGGGD WSAEDEEAFK
     APIRDQYEAQ GNPYYSTARL WDDGVIDPAD TRQVLGLALS AAANAPLEPV RYGVFRM
//