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
//