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Database: UniProt
Entry: P43873
LinkDB: P43873
Original site: P43873 
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   05-DEC-2018, entry version 130.
DE   RecName: Full=Biotin carboxylase;
DE            EC=6.3.4.14;
DE   AltName: Full=Acetyl-CoA carboxylase subunit A;
DE            Short=ACC;
DE            EC=6.4.1.2;
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.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
CC         = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:456216; EC=6.4.1.2;
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin
CC       carboxyl carrier protein, biotin carboxylase and the two subunits
CC       of carboxyl transferase in a 2:2 complex. {ECO:0000250}.
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   PDBsum; 4MV1; -.
DR   PDBsum; 4MV3; -.
DR   PDBsum; 4MV4; -.
DR   PDBsum; 4MV6; -.
DR   PDBsum; 4MV7; -.
DR   PDBsum; 4MV8; -.
DR   PDBsum; 4MV9; -.
DR   PDBsum; 4RZQ; -.
DR   ProteinModelPortal; P43873; -.
DR   SMR; P43873; -.
DR   STRING; 71421.HI0972; -.
DR   PRIDE; P43873; -.
DR   EnsemblBacteria; AAC22632; AAC22632; HI_0972.
DR   GeneID; 949398; -.
DR   KEGG; hin:HI0972; -.
DR   PATRIC; fig|71421.8.peg.1013; -.
DR   eggNOG; ENOG4105CER; Bacteria.
DR   eggNOG; COG0439; LUCA.
DR   KO; K01961; -.
DR   OMA; FVEICSH; -.
DR   PhylomeDB; P43873; -.
DR   BioCyc; HINF71421:G1GJ1-1013-MONOMER; -.
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:InterPro.
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; Complete proteome;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
KW   Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    448       Biotin carboxylase.
FT                                /FTId=PRO_0000146793.
FT   DOMAIN        1    445       Biotin carboxylation.
FT   DOMAIN      120    317       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   ACT_SITE    292    292       {ECO:0000255}.
FT   BINDING     116    116       ATP. {ECO:0000250}.
FT   BINDING     201    201       ATP. {ECO:0000250}.
FT   BINDING     236    236       ATP. {ECO:0000250}.
FT   STRAND        4      7       {ECO:0000244|PDB:4MV4}.
FT   HELIX        11     24       {ECO:0000244|PDB:4MV4}.
FT   STRAND       27     33       {ECO:0000244|PDB:4MV4}.
FT   HELIX        34     36       {ECO:0000244|PDB:4MV4}.
FT   HELIX        40     44       {ECO:0000244|PDB:4MV4}.
FT   STRAND       45     55       {ECO:0000244|PDB:4MV4}.
FT   HELIX        56     58       {ECO:0000244|PDB:4MV4}.
FT   TURN         59     61       {ECO:0000244|PDB:4MV4}.
FT   HELIX        63     73       {ECO:0000244|PDB:4MV4}.
FT   STRAND       76     79       {ECO:0000244|PDB:4MV4}.
FT   TURN         84     87       {ECO:0000244|PDB:4MV4}.
FT   HELIX        89     97       {ECO:0000244|PDB:4MV4}.
FT   STRAND      101    104       {ECO:0000244|PDB:4MV4}.
FT   HELIX       107    114       {ECO:0000244|PDB:4MV4}.
FT   HELIX       116    126       {ECO:0000244|PDB:4MV4}.
FT   HELIX       142    152       {ECO:0000244|PDB:4MV4}.
FT   STRAND      154    160       {ECO:0000244|PDB:4MV4}.
FT   STRAND      169    172       {ECO:0000244|PDB:4MV4}.
FT   HELIX       175    192       {ECO:0000244|PDB:4MV4}.
FT   STRAND      198    202       {ECO:0000244|PDB:4MV4}.
FT   STRAND      208    216       {ECO:0000244|PDB:4MV4}.
FT   STRAND      222    234       {ECO:0000244|PDB:4MV4}.
FT   STRAND      237    244       {ECO:0000244|PDB:4MV4}.
FT   HELIX       250    267       {ECO:0000244|PDB:4MV4}.
FT   STRAND      271    280       {ECO:0000244|PDB:4MV4}.
FT   STRAND      283    290       {ECO:0000244|PDB:4MV4}.
FT   HELIX       297    304       {ECO:0000244|PDB:4MV4}.
FT   HELIX       308    316       {ECO:0000244|PDB:4MV4}.
FT   HELIX       325    327       {ECO:0000244|PDB:4MV4}.
FT   STRAND      332    342       {ECO:0000244|PDB:4MV4}.
FT   TURN        344    346       {ECO:0000244|PDB:4MV4}.
FT   STRAND      356    358       {ECO:0000244|PDB:4MV4}.
FT   STRAND      365    368       {ECO:0000244|PDB:4MV4}.
FT   STRAND      379    381       {ECO:0000244|PDB:4MV4}.
FT   STRAND      384    394       {ECO:0000244|PDB:4MV4}.
FT   HELIX       395    408       {ECO:0000244|PDB:4MV4}.
FT   STRAND      410    414       {ECO:0000244|PDB:4MV4}.
FT   HELIX       418    425       {ECO:0000244|PDB:4MV4}.
FT   HELIX       428    432       {ECO:0000244|PDB:4MV4}.
FT   HELIX       439    444       {ECO:0000244|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
//
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