ID   H5U1X1_9ACTN            Unreviewed;       532 AA.
AC   H5U1X1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Acyl-CoA carboxylase beta chain {ECO:0000313|EMBL:GAB39729.1};
GN   Name=accD {ECO:0000313|EMBL:GAB39729.1};
GN   ORFNames=GOSPT_075_00880 {ECO:0000313|EMBL:GAB39729.1};
OS   Gordonia sputi NBRC 100414.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1089453 {ECO:0000313|EMBL:GAB39729.1, ECO:0000313|Proteomes:UP000005845};
RN   [1] {ECO:0000313|EMBL:GAB39729.1, ECO:0000313|Proteomes:UP000005845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100414 {ECO:0000313|EMBL:GAB39729.1,
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:GAB39729.1}.
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DR   EMBL; BAFC01000075; GAB39729.1; -; Genomic_DNA.
DR   RefSeq; WP_005206601.1; NZ_BAFC01000075.1.
DR   AlphaFoldDB; H5U1X1; -.
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: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;
FT   DOMAIN          22..273
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          280..518
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   532 AA;  57120 MW;  0029CFC9F56FC861 CRC64;
     MTALRSTIDS TSDDFTAARD SMLEKLDQIH GELDKALAGG GDKYVERHRK RGKMTARERI
     EMLLDEDSDF LELCPLAAYG SDFHVGASVV VGIGVVEGVE CLVVASDPTV KGGTSNPWTL
     RKTLRANDIA MQNRLPVISL VESGGADLPT QKEVFVPGGR MFRDLTRLSA AGIPTIALVF
     GNSTAGGAYI PGMSDHVVMI DGRSKVFLGG PPLVKMATGE ESDDESLGGA QMHARTSGLA
     DYYAADEQDA IRIGRRIVSR LNWTKAGGQP RAQVREPRYD PEELLGIVPP DLKIPFNPRD
     VIARVVDDSD FDEFKPEYGN SLCTGWADIH GYPVGILANA QGVLFSQEAQ KATQFIELAN
     RSNTPLLFLH NTTGYMVGKE YEQNGIIKHG AMMINAVSNS KVPHLSVLMG ASYGAGHYGM
     CGRAYDPRFL FAWPSAKSAV MGAAQLAGVI SIVSRAATEA RGGTVDEAAD AGMRQMIEAQ
     IEAESVPAFL SGMLYDDGVI DPRDTRTVLG LCLSAIHNGP VEGTSSFGVF RM
//