ID D1A9A0_THECD Unreviewed; 500 AA.
AC D1A9A0;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Carboxyl transferase {ECO:0000313|EMBL:ACY96796.1};
GN OrderedLocusNames=Tcur_1213 {ECO:0000313|EMBL:ACY96796.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY96796.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY96796.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
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DR EMBL; CP001738; ACY96796.1; -; Genomic_DNA.
DR RefSeq; WP_012851580.1; NC_013510.1.
DR AlphaFoldDB; D1A9A0; -.
DR STRING; 471852.Tcur_1213; -.
DR KEGG; tcu:Tcur_1213; -.
DR eggNOG; COG0777; Bacteria.
DR eggNOG; COG0825; Bacteria.
DR HOGENOM; CLU_015486_2_1_11; -.
DR OrthoDB; 9772975at2; -.
DR Proteomes; UP000001918; Chromosome.
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:UP000001918};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACY96796.1}.
FT DOMAIN 1..237
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 251..477
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 227..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 51920 MW; F3A0570242BA532B CRC64;
MTRIGARELI GRILDAGRWT SWDTPPRRVA APGSAYEAEL AAARERTGCD EAVITGEGLL
RGRRVAFVVS EFGFLAGSIG LATADRIVAA VERATAERLP LLAAPSSGGT RMQEGTAAFV
QMARITAAVM RHRAAGLPYL VYLRHPTTGG VLASWGSLGH VTAAEPGALI GFLGPRVYEA
LHGEPFPPGV QVAENLAAKG VVDAVVGIDE LPDVAARALS VLCAGQAPAR GGRPRPAAPE
PAADDTPAWE SIERSRRADR PGVRELLRYG ARDVTVLSGT GEGEADPGLL LALARFGEAA
CVVVGQDRRS QRSGHPIGPA GLRVARRGMR LARELHLPLL TVVDTPGAVL SAEAEERGLA
GEIARCLAEL TTLPGPTLCV LLGEGTGGAA LALLPTDRVL CARHGWLSPL PPEGASVIVH
RTTARAAEMA QAQGVRSADL LAAGIADHLL PECPDAAAEP RAFCTRTAAA IAAHLAELTA
ADPADRMAAR DRRLQGPPPA
//