ACCC_HAEIN
ID ACCC_HAEIN Reviewed; 448 AA.
AC P43873;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 144.
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; OrderedLocusNames=HI_0972;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2] {ECO:0007744|PDB:4MV1, ECO:0007744|PDB:4MV3, ECO:0007744|PDB:4MV4, ECO:0007744|PDB:4MV6, ECO:0007744|PDB:4MV7, ECO:0007744|PDB:4MV8, ECO:0007744|PDB:4MV9, ECO:0007744|PDB:4RZQ}
RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) IN COMPLEX WITH ADP; ATP ANALOGS AND
RP MAGNESIUM.
RX PubMed=26020841; DOI=10.1021/acs.biochem.5b00340;
RA Broussard T.C., Pakhomova S., Neau D.B., Bonnot R., Waldrop G.L.;
RT "Structural Analysis of Substrate, Reaction Intermediate, and Product
RT Binding in Haemophilus influenzae Biotin Carboxylase.";
RL Biochemistry 54:3860-3870(2015).
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; L42023; AAC22632.1; -; Genomic_DNA.
DR PIR; F64105; F64105.
DR RefSeq; NP_439133.1; NC_000907.1.
DR RefSeq; WP_005655956.1; NC_000907.1.
DR PDB; 4MV1; X-ray; 1.91 A; A=1-448.
DR PDB; 4MV3; X-ray; 1.69 A; A=1-448.
DR PDB; 4MV4; X-ray; 1.61 A; A=1-448.
DR PDB; 4MV6; X-ray; 1.77 A; A=1-448.
DR PDB; 4MV7; X-ray; 1.73 A; A=1-448.
DR PDB; 4MV8; X-ray; 2.06 A; A=1-448.
DR PDB; 4MV9; X-ray; 1.98 A; A=1-448.
DR PDB; 4RZQ; X-ray; 1.98 A; A=1-448.
DR PDB; 6OI8; X-ray; 2.50 A; A=1-448.
DR PDB; 6OJH; X-ray; 2.05 A; A=1-448.
DR PDBsum; 4MV1; -.
DR PDBsum; 4MV3; -.
DR PDBsum; 4MV4; -.
DR PDBsum; 4MV6; -.
DR PDBsum; 4MV7; -.
DR PDBsum; 4MV8; -.
DR PDBsum; 4MV9; -.
DR PDBsum; 4RZQ; -.
DR PDBsum; 6OI8; -.
DR PDBsum; 6OJH; -.
DR AlphaFoldDB; P43873; -.
DR SMR; P43873; -.
DR STRING; 71421.HI_0972; -.
DR EnsemblBacteria; AAC22632; AAC22632; HI_0972.
DR KEGG; hin:HI_0972; -.
DR PATRIC; fig|71421.8.peg.1013; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_6; -.
DR OMA; FVEICSH; -.
DR PhylomeDB; P43873; -.
DR BioCyc; HINF71421:G1GJ1-1013-MON; -.
DR BRENDA; 6.3.4.14; 2529.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000000579; 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; 3.30.1490.20; -; 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 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 SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR00514; accC; 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..448
FT /note="Biotin carboxylase"
FT /id="PRO_0000146793"
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:0000269|PubMed:26020841,
FT ECO:0007744|PDB:4MV8"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:26020841,
FT ECO:0007744|PDB:4MV3, ECO:0007744|PDB:4MV4"
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:0000269|PubMed:26020841,
FT ECO:0007744|PDB:4MV1, ECO:0007744|PDB:4MV3,
FT ECO:0007744|PDB:4MV4, ECO:0007744|PDB:4MV8,
FT ECO:0007744|PDB:4RZQ"
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:0000269|PubMed:26020841,
FT ECO:0007744|PDB:4MV3, ECO:0007744|PDB:4MV4"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26020841,
FT ECO:0007744|PDB:4MV4"
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:0000269|PubMed:26020841,
FT ECO:0007744|PDB:4MV3, ECO:0007744|PDB:4MV4"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26020841,
FT ECO:0007744|PDB:4MV4"
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:0000269|PubMed:26020841,
FT ECO:0007744|PDB:4MV4"
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 4..7
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 45..55
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:4MV4"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:4MV4"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 175..192
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 222..234
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 250..267
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 271..280
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 308..316
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 332..342
FT /evidence="ECO:0007829|PDB:4MV4"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 384..394
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 395..408
FT /evidence="ECO:0007829|PDB:4MV4"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 418..425
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:4MV4"
FT HELIX 439..444
FT /evidence="ECO:0007829|PDB:4MV4"
SQ SEQUENCE 448 AA; 49108 MW; 2B497E2A31ED96D1 CRC64;
MLEKVVIANR GEIALRILRA CKELGIKTVA VHSTADRDLK HVLLADETIC IGPAPSAKSY
LNIPAIIAAA EVTGADAIHP GYGFLSENAD FAEQVERSGF TFIGPTADVI RLMGDKVSAI
KAMKKAGVPC VPGSDGPVSN DIAKNKEIAK RIGYPIIIKA SGGGGGRGMR VVRSEDALEE
SIAMTKAEAK AAFNNDMVYM EKYLENPRHV EIQVLADTHG NAVYLAERDC SMQRRHQKVV
EEAPAPGITE EVRRDIGSRC ANACVEIGYR GAGTFEFLYE NGEFYFIEMN TRIQVEHPVT
EMITGVDLVK EQLRIAAGLP ISFKQEDIKV KGHAMECRIN AEDPKTFLPS PGKVNHLHSP
GGLGVRWDSH VYGGYTVPPH YDSMIAKLIT YGDTREVAIR RMQNALSETI IDGIKTNIPL
HELILEDENF QKGGTNIHYL EKKLGMNE
