ID ACCC_PSEAE Reviewed; 449 AA.
AC P37798;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=Biotin carboxylase;
DE EC=6.3.4.14 {ECO:0000250|UniProtKB:P24182};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000305};
GN Name=accC; Synonyms=fabG; OrderedLocusNames=PA4848;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=7693652; DOI=10.1128/jb.175.21.6881-6889.1993;
RA Best E.A., Knauf V.C.;
RT "Organization and nucleotide sequences of the genes encoding the biotin
RT carboxyl carrier protein and biotin carboxylase protein of Pseudomonas
RT aeruginosa acetyl coenzyme A carboxylase.";
RL J. Bacteriol. 175:6881-6889(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC carboxylase complex; first, biotin carboxylase catalyzes the
CC carboxylation of the carrier protein and then the transcarboxylase
CC transfers the carboxyl group to form malonyl-CoA.
CC {ECO:0000250|UniProtKB:P24182}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000250|UniProtKB:P24182};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000250|UniProtKB:P24182}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl
CC carrier protein, biotin carboxylase and the two subunits of carboxyl
CC transferase in a 2:2 complex. {ECO:0000250|UniProtKB:P24182}.
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DR EMBL; L14612; AAA16041.1; -; Unassigned_DNA.
DR EMBL; AE004091; AAG08233.1; -; Genomic_DNA.
DR PIR; B49342; B49342.
DR RefSeq; NP_253535.1; NC_002516.2.
DR RefSeq; WP_003095391.1; NZ_QZGE01000002.1.
DR PDB; 2C00; X-ray; 2.50 A; A/B=1-449.
DR PDB; 2VQD; X-ray; 2.41 A; A=1-449.
DR PDBsum; 2C00; -.
DR PDBsum; 2VQD; -.
DR AlphaFoldDB; P37798; -.
DR SMR; P37798; -.
DR STRING; 208964.PA4848; -.
DR BindingDB; P37798; -.
DR ChEMBL; CHEMBL4523221; -.
DR PaxDb; 208964-PA4848; -.
DR GeneID; 77223396; -.
DR GeneID; 879558; -.
DR KEGG; pae:PA4848; -.
DR PATRIC; fig|208964.12.peg.5080; -.
DR PseudoCAP; PA4848; -.
DR HOGENOM; CLU_000395_3_2_6; -.
DR InParanoid; P37798; -.
DR OrthoDB; 9763189at2; -.
DR PhylomeDB; P37798; -.
DR BioCyc; PAER208964:G1FZ6-4962-MONOMER; -.
DR UniPathway; UPA00655; UER00711.
DR EvolutionaryTrace; P37798; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR00514; accC; 1.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 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; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SMART; SM01209; GARS_A; 1.
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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biotin; Fatty acid biosynthesis;
KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..449
FT /note="Biotin carboxylase"
FT /id="PRO_0000146794"
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT ACT_SITE 292
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 165..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 201..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 238
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 276
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 290
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 292
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 295
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 338
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 338
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2VQD"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:2VQD"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2C00"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 178..193
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 208..220
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 250..267
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 270..280
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 308..316
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 332..342
FT /evidence="ECO:0007829|PDB:2VQD"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 383..394
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 395..408
FT /evidence="ECO:0007829|PDB:2VQD"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 418..424
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:2VQD"
FT HELIX 439..444
FT /evidence="ECO:0007829|PDB:2VQD"
SQ SEQUENCE 449 AA; 48888 MW; 3B04C77785C73541 CRC64;
MLEKVLIANR GEIALRILRA CKELGIKTVA VHSTADRELM HLSLADESVC IGPAPATQSY
LQIPAIIAAA EVTGATAIHP GYGFLAENAD FAEQIERSGF TFVGPTAEVI RLMGDKVSAK
DAMKRAGVPT VPGSDGPLPE DEETALAIAR EVGYPVIIKA AGGGGGRGMR VVYDESELIK
SAKLTRTEAG AAFGNPMVYL EKFLTNPRHV EVQVLSDGQG NAIHLGDRDC SLQRRHQKVI
EEAPAPGIDE KARQEVFARC VQACIEIGYR GAGTFEFLYE NGRFYFIEMN TRVQVEHPVS
EMVTGVDIVK EMLRIASGEK LSIRQEDVVI RGHALECRIN AEDPKTFMPS PGKVKHFHAP
GGNGVRVDSH LYSGYSVPPN YDSLVGKVIT YGADRDEALA RMRNALDELI VDGIKTNTEL
HKDLVRDAAF CKGGVNIHYL EKKLGMDKH
//
