ID D7AXW9_NOCDD Unreviewed; 497 AA.
AC D7AXW9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Carboxyl transferase {ECO:0000313|EMBL:ADH68023.1};
GN OrderedLocusNames=Ndas_2606 {ECO:0000313|EMBL:ADH68023.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH68023.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH68023.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
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DR EMBL; CP002040; ADH68023.1; -; Genomic_DNA.
DR RefSeq; WP_013153630.1; NC_014210.1.
DR AlphaFoldDB; D7AXW9; -.
DR STRING; 446468.Ndas_2606; -.
DR KEGG; nda:Ndas_2606; -.
DR eggNOG; COG0777; Bacteria.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_2_1_11; -.
DR OrthoDB; 9772975at2; -.
DR Proteomes; UP000002219; Chromosome 1.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR PANTHER; PTHR42995; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR PANTHER; PTHR42995:SF5; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR PRINTS; PR01070; ACCCTRFRASEB.
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:UP000002219};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADH68023.1}.
FT DOMAIN 1..237
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 222..473
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 223..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..241
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 51526 MW; 3FEA28671603554C CRC64;
METRDTAREL LDRTLDAGSH VSWDEAPLDV DPDPAYADAL TRARAATGCD EAVLTGEGRL
HGRRVAVVAS EFGFLAGSVG LAAAARIVAA VERATAERLP LLAAPASGGT RMQEGTPAFV
AMAAITAAVT AHKAAGLPYL VYLRHPTTGG VLASWGSLGH LTAAEPGALV GFLGPRVYEA
LHGAPFPEGV QRAENLQRHG LVDAVLPPDR LRDAAGLALD VLLDRPDPAT PPPPPAEPDS
PAPVWDSVTR SRRKERPGVR ELLRHAASHV VRLRGSGEGE ASPALVTALA RFGGRPCVLV
GQDRSRQSAE QPMGPDALRE ARRGMRLAAE LRLPLVTVID TPGAALSADA EERGTAGQIA
RCLAEMTSLA APTVSVLLGE GTGGGAIALL PADRVLCAQH AWLAPLPPEG ASAIVHRTPD
RAGELAEAQG IGSADLRARG LVDRVVPEFG DAADEDGAFC ARMGEAIARE LAAVQPSGDA
EPPAGRAARY RRLCAAP
//