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Database: UniProt
Entry: N0E4F2_9MICO
LinkDB: N0E4F2_9MICO
Original site: N0E4F2_9MICO 
ID   N0E4F2_9MICO            Unreviewed;       501 AA.
AC   N0E4F2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Putative Acetyl-coenzyme A carboxylase carboxyl transferase subunits beta/alpha {ECO:0000313|EMBL:CCH69879.1};
DE            EC=6.4.1.2 {ECO:0000313|EMBL:CCH69879.1};
GN   ORFNames=BN10_430005 {ECO:0000313|EMBL:CCH69879.1};
OS   Phycicoccus elongatus Lp2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Phycicoccus.
OX   NCBI_TaxID=1193181 {ECO:0000313|EMBL:CCH69879.1, ECO:0000313|Proteomes:UP000013167};
RN   [1] {ECO:0000313|EMBL:CCH69879.1, ECO:0000313|Proteomes:UP000013167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lp2 {ECO:0000313|EMBL:CCH69879.1,
RC   ECO:0000313|Proteomes:UP000013167};
RX   PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA   Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA   Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA   Nielsen K.L., Nielsen P.H.;
RT   "A metabolic model for members of the genus Tetrasphaera involved in
RT   enhanced biological phosphorus removal.";
RL   ISME J. 7:543-554(2013).
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:CCH69879.1}.
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DR   EMBL; CAIZ01000112; CCH69879.1; -; Genomic_DNA.
DR   RefSeq; WP_010849755.1; NZ_HF570956.1.
DR   AlphaFoldDB; N0E4F2; -.
DR   STRING; 1193181.BN10_430005; -.
DR   eggNOG; COG0777; Bacteria.
DR   eggNOG; COG0825; Bacteria.
DR   HOGENOM; CLU_015486_2_1_11; -.
DR   OrthoDB; 9772975at2; -.
DR   Proteomes; UP000013167; Unassembled WGS sequence.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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   Ligase {ECO:0000313|EMBL:CCH69879.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013167};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCH69879.1}.
FT   DOMAIN          1..242
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          236..478
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   501 AA;  52919 MW;  55A7A0AB10B1C773 CRC64;
     MSEPPPRRLG ARALFEAVLD EGTFGSWDNA PLPVAADGSA YAAELAEAAA KAGTDESVIT
     GEGRIGGRRV ALIAGEFRFL AGSIGRTSAE RVVLAFERAT REGLPLFAAP SSGGTRMQEG
     TPAFVTMVKI SAAVAAFKAA KLPYITYLRH PTTGGVFASW GSLGHVTVAE PGATIGFLGA
     RVYEALYGQP FPEGVQTAEN LYEHGLLDAV LPVEGLAQVA GRFLDLVLAP RSPEVVADVP
     IEPLEEVDAW TSIAASRRPD RPGVRELLRY GAHDVLPLFG TGAGEWDRSL FLALARFGEV
     PCVVLGQDRR RETPEKPLSP SGLRVARRGM RLATELDLPL VSIIDTSGAA LSREAEEGGL
     AGEIARCLAE LVVLAEPTLG VLLGQGTGGG ALALMPADRV ISAQHSWLSP LPPEGASAIL
     YRDTAHAPEL AAQQRVRSTD LLADGIVHRI VAERPDAADE PEAFCQRLAQ VIAHELGELS
     AMKPASRLAA RHSRYRNLGL G
//
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