ID A0A1E7KIA6_9ACTN Unreviewed; 531 AA.
AC A0A1E7KIA6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Methylmalonyl-CoA carboxyltransferase {ECO:0000313|EMBL:OEV03660.1};
GN ORFNames=AN216_10410 {ECO:0000313|EMBL:OEV03660.1};
OS Streptomyces oceani.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1075402 {ECO:0000313|EMBL:OEV03660.1, ECO:0000313|Proteomes:UP000176101};
RN [1] {ECO:0000313|EMBL:OEV03660.1, ECO:0000313|Proteomes:UP000176101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 02100 {ECO:0000313|EMBL:OEV03660.1,
RC ECO:0000313|Proteomes:UP000176101};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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:OEV03660.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJGU01000116; OEV03660.1; -; Genomic_DNA.
DR RefSeq; WP_070196355.1; NZ_LJGU01000116.1.
DR AlphaFoldDB; A0A1E7KIA6; -.
DR STRING; 1075402.AN216_10410; -.
DR PATRIC; fig|1075402.3.peg.2916; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000176101; Unassembled WGS sequence.
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; PTHR43842:SF2; BIOTIN-DEPENDENT ACETYL-_PROPIONYL-COENZYME A CARBOXYLASE BETA5 SUBUNIT; 1.
DR PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 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:UP000176101};
KW Transferase {ECO:0000313|EMBL:OEV03660.1}.
FT DOMAIN 13..269
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 278..513
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 57623 MW; 4FC48669DB687C88 CRC64;
MSEQESSPDI HTTAGKIADF QRRTAEAVHA GSERAVEKQH AKGKLTARER VELLLDEGSF
TELDEFARHR STAFGIERNR PYGDGVVTGY GTVDGRPVCV YSQDFTIFGG SLGEVYGEKI
VKVMDFAMRT GCPVIGINDG GGARIQEGVT ALGLFAEIFR RNVHASGVIP QISLIMGPCA
GGAVYSPAIT DFTVMVDQSS HMFITGPDVI KTVTGEDVGF EELGGARTHN TTSGVAHHLA
GDEKDAIDHV KALLSYLPSN NLSEPPVFPE EADLETSDED RELDTLIPDS ANQPYDMHSA
IEHVLDDSEF LENQPLFAPN IITGFGRVEG QSVGVVANQP MQLAGCLDID ASEKAARFVR
TCDAYNIPVL TFVDVPGFLP GTDQEYDGII RRGAKLIFAY AEATVPLITV ITRKAFGGAY
DVMGSKHLGA DLNFAWPTAQ IAVMGAQGAV NILHRKRLAD AGSPERTEEL RAELTQEYED
TLLNPYVAAE RGYVDAVIMP SETRRHITRG LRTLRTKRAQ LPPKKHGNIP L
//