ID   H5U3D9_9ACTN            Unreviewed;       544 AA.
AC   H5U3D9;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Acyl-CoA carboxylase beta chain {ECO:0000313|EMBL:GAB40247.1};
GN   Name=accD {ECO:0000313|EMBL:GAB40247.1};
GN   ORFNames=GOSPT_095_00370 {ECO:0000313|EMBL:GAB40247.1};
OS   Gordonia sputi NBRC 100414.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1089453 {ECO:0000313|EMBL:GAB40247.1, ECO:0000313|Proteomes:UP000005845};
RN   [1] {ECO:0000313|EMBL:GAB40247.1, ECO:0000313|Proteomes:UP000005845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100414 {ECO:0000313|EMBL:GAB40247.1,
RC   ECO:0000313|Proteomes:UP000005845};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia sputi NBRC 100414.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC       {ECO:0000256|ARBA:ARBA00006102}.
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:GAB40247.1}.
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DR   EMBL; BAFC01000093; GAB40247.1; -; Genomic_DNA.
DR   AlphaFoldDB; H5U3D9; -.
DR   eggNOG; COG4799; Bacteria.
DR   Proteomes; UP000005845; 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   3: Inferred from homology;
FT   DOMAIN          31..287
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          293..536
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   544 AA;  58109 MW;  2DFB1C89B23C92FD CRC64;
     MVSTSSTSEK GSTSGEGSGG GNGSASGRAV HEANVATLRE RLARVAVGGG ERARERHISR
     GKLLPRDRVD GLLDVGSPFL EVGPLAAFGM YDDKAPSAGV IAGVGRVAGR ECMIVANDAT
     VSGGTYYPMT VKKHLRAQEI AAANRLPCIY LVDSGGAMLL AQDEVFPDRE HFGRIFYNQA
     TMSAAGIPQI AAVLGSSTAG GAYVPAMSDE TVIVRNQGTI FLAGPPLVKA ATGEDVSAED
     LGGGAMHSSV SGVTDHLVDN DQQALAKVRE IIATLGPREQ PQWDTIAPRE PARSQTDIYD
     VVPTDARTPY DVRQVIEIIS DAGEFTEFKA NYGTTLVTAF AHVHGHPVGF VANNGVLFSE
     SALKGAHFIE LCDQRRIPLV FLQNITGFMV GRAYEEGGIA KNGAKMVNAV ACARVPKFTV
     MIGGSFGAGN YSMCGRAYSP RFLWSWPNAR ISVMGGPQAA DTLATVRRNQ IERSGKEWSA
     DDEEAFKTPI REQFDEQSDA YYSTARLWDD GIVDPAHTRT LLGLALETAR YAPLADQRYG
     VFRM
//