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Database: UniProt
Entry: V9XFI4_9NOCA
LinkDB: V9XFI4_9NOCA
Original site: V9XFI4_9NOCA 
ID   V9XFI4_9NOCA            Unreviewed;      1060 AA.
AC   V9XFI4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE            EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
GN   ORFNames=Y013_17070 {ECO:0000313|EMBL:AHD22226.1};
OS   Rhodococcus pyridinivorans SB3094.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD22226.1, ECO:0000313|Proteomes:UP000018781};
RN   [1] {ECO:0000313|EMBL:AHD22226.1, ECO:0000313|Proteomes:UP000018781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB3094 {ECO:0000313|EMBL:AHD22226.1,
RC   ECO:0000313|Proteomes:UP000018781};
RX   PubMed=24874690;
RA   Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA   Nielsen P.H., Nielsen J.L.;
RT   "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT   Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL   Genome Announc. 2:e00525-14(2014).
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}.
CC   -!- SIMILARITY: Belongs to the AccD/PCCB family.
CC       {ECO:0000256|ARBA:ARBA00006102}.
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DR   EMBL; CP006996; AHD22226.1; -; Genomic_DNA.
DR   RefSeq; WP_024102625.1; NC_023150.1.
DR   AlphaFoldDB; V9XFI4; -.
DR   GeneID; 29939378; -.
DR   KEGG; rpy:Y013_17070; -.
DR   PATRIC; fig|1435356.3.peg.3444; -.
DR   eggNOG; COG0439; Bacteria.
DR   eggNOG; COG4799; Bacteria.
DR   HOGENOM; CLU_009218_0_0_11; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000018781; Chromosome.
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:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
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; 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; PTHR48095:SF5; BLL7292 PROTEIN; 1.
DR   PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 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; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          1..460
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          116..313
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          468..548
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          567..826
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          818..1060
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   1060 AA;  111847 MW;  48F23EBE9D85C9A7 CRC64;
     MLLVANRGEI ALRVVRTAGD LGLDTVAVHA ADDADAPHVR AATRAEALPE SGPSAYLDPG
     AIIGVARATG CTLVHPGYGF LSENAAFAQA CADAGLTFVG PSPEALRVLG DKRAARSVAE
     ELGIPVTAAV ETTDPESVRA FLRDRPGGIV VKALSGGGGR GMRVVRDAAD LDEALRLAAA
     EAHAAFDDDR LYAEVLVERA RHVEVQVVAA ESGSGTRAVA LGDRDCSVQR RHQKLVEIAP
     APDLPDALRE ALHGAAVRLI GHVGCHGLST VEFLVHDDGF VFLEVNPRIQ VEHTVTEEVT
     GVDLVATQIA VARGTGFDEL GLPKGITFDG KKIGGRPAAA QGIAVQVRVN AETPRADGIA
     LPTAGTLTAF TPPTGPGIRV DTHGRPGLEV TGRYDSLLAK VVAYVRSGDR VAVLRKASTA
     LGEFIVDGVG TNRDLLQKIL DDKEFRSGNV RTTWLGERLA DFVDTAPTAP VEYTDLRADE
     QAVHAEMVGT VVEIARAGDT VPAGAPLAVL DAMKMQHEIR APGSAVVERV LVEPGRTVEP
     GTVLAVVRVL DTDTATDDIA AADLDADRAD LDEIRRRHEV TTDAARPEIV AKRHGRGRRT
     ARENIADLVD DGSFVEYGPL VLAAQRGRRS EEDLIANTPA DGLVGGTARI GGAEVVVMSY
     DYTVLAGTQG RNNHRKTDRL LELAARRRVP LVLFAEGGGG RPGDVDAGSG AGLDLTTFRS
     MASLRGRVPT VAVVSGRCFA GNAALAGVCD VLIATPDANI GMGGPAMIEG GGLGVHRPED
     IGPIDVQRRN GVVHVAARDE AHAVDVARRY LAYFTAPHED RQAPDPRLAR HVVPENRLRA
     YDVRSAIDAI ADLGSVLELR PDYGVGIVTA LMRVEGASYG VLANSSAHLG GAIDAEAADK
     AADFLELCES HRLPVVSLCD TPGFMVGPES EKDATVRRFG RFFVAGARLT VPFGMIILRK
     GYGLGAMAMA GGSFHAPEFT VAWPTGEIGG MGLEGAVRLG FRKELDAAET PREREELFGR
     LVALAYQQGK ALQAATSFEL DDVIDPADSR AWIERLVQPR
//
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