ID Q13I48_PARXL Unreviewed; 1033 AA.
AC Q13I48;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
GN ORFNames=Bxe_C0325 {ECO:0000313|EMBL:ABE36241.1};
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE36241.1, ECO:0000313|Proteomes:UP000001817};
RN [1] {ECO:0000313|EMBL:ABE36241.1, ECO:0000313|Proteomes:UP000001817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400 {ECO:0000313|EMBL:ABE36241.1,
RC ECO:0000313|Proteomes:UP000001817};
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
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DR EMBL; CP000272; ABE36241.1; -; Genomic_DNA.
DR RefSeq; WP_011493501.1; NZ_CP008761.1.
DR AlphaFoldDB; Q13I48; -.
DR STRING; 266265.Bxe_C0325; -.
DR KEGG; bxb:DR64_8108; -.
DR KEGG; bxe:Bxe_C0325; -.
DR PATRIC; fig|266265.5.peg.8102; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG4799; Bacteria.
DR OrthoDB; 9803706at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001817; Chromosome 3.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABE36241.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 1..437
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 118..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 432..509
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 514..787
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 788..1019
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1033 AA; 109127 MW; 298FFFFA914FA942 CRC64;
MSRVLIANRG EVAVRIVRAA KSVGLQTVGI HTPEEANALH VRDSDIAVAL AGVGTAAYLD
IASIIAAAVR TNCSFIHPGY GFLSESAAFA RACEQAGVTF IGPSPDTLDV FGDKASTREL
AIRLDVPVLP ATAGLADDAS ALSFMQSLAA PVIVKAVAGG GGRGMRIVTD PTDLPAALSR
CRSEAERGFG RDDVYVERYL PRSRHIEVQV IGDGSSVVHL GTRDCSLQSR HQKVIEIAPA
PWLPVEIEEA LLEHALQLAR AVQYRGAGTM EFLIDVDNPS HYYFIEGNPR LQVEHGITEL
VTGLDIVALQ FAIARGRSLA DEGITQDNVV TSGVAVEARV TLTTPGTIAR FVSPGKGRVD
SGAYDGLAVG SGFDPLLAKV MVHEPDYPRC ICALADSLGE LVVEGPATNR DGLLSLLADP
RVRAGDITTT LIDDLPAASA TALVSKVAGS VIAVLARPGE PLRRGQPIVV VEAMKMEHEV
VAPAAGRLEE MLVAVGQQIT TGQRVASMGY SGAEAEHDAA PGEPAARADL AENLRRHSIT
LDEARPEAVA SRHARHKRTA RENVADLVDP GSFVEYGALV IAAQRRRRTV EDLELNTPAD
GLVAGFGTVN GQQIAVLAYD YSVLAGTQGV QSHKKAERLF ELARRRHAPV VIFAEGGGGR
PGDIDNAAKA TGMDLGTFVA LGRLNGRVPT VAIASGRCFA GNAALVGACD LVIATADANI
GMGGPAMIEG GGLGRVESRD IGPAARQFEN GVVDVLVADE AEATASAKKY LSYFHAAKRN
WTAGEQQHLR TIVPEARSRP FDVLRVIQVL SDDDAVLELR AGFGRGIITC LVRIEGVAIG
IVANNGLHLG GAIDSDSADK MARFLALCDT YSLPIVSLCD TPGFMVGPAS EETAAVRHFG
RLLVAGPNLS VPLCTVVIRK AWGLGGQAMA GGGFRVPDAI VAWPTAEFGA MGPEGAVRLG
FRRELEAIAD PVARDAEFDR LVKDYVRDGR GYNAASAFEI DDVIDPADTR RWILATVNRA
EPIPPTRRHL DTW
//
