GENTAUR Molecular Products.

 ACAC_SCHPO              Reviewed;        2280 AA.
 P78820; O94557; Q09447; Q09576; Q09616; Q09667;
 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
 11-JAN-2001, sequence version 2.
 12-SEP-2018, entry version 169.
 RecName: Full=Acetyl-CoA carboxylase;
          Short=ACC;
          EC=6.4.1.2;
 AltName: Full=Cell untimely torn protein 6;
 Includes:
   RecName: Full=Biotin carboxylase;
            EC=6.3.4.14;
 Name=cut6; ORFNames=SPAC56E4.04c;
 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
 Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
 Schizosaccharomycetes; Schizosaccharomycetales;
 Schizosaccharomycetaceae; Schizosaccharomyces.
 NCBI_TaxID=284812;
 [1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 STRAIN=972 / HM123;
 Saito A., Kazuta Y., Toh H., Kondo H., Tanabe T.;
 "Biotin-dependent enzymes in Schizosaccharomyces pombe: cloning and
 nucleotide sequences of acetyl-CoA carboxylase and pyruvate
 carboxylase.";
 Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=972 / ATCC 24843;
 PubMed=11859360; DOI=10.1038/nature724;
 Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
 Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
 Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
 Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
 Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
 Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
 James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
 Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
 Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
 Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
 Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
 Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
 Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
 Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
 Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
 Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
 Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
 Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
 Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
 Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
 Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
 Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
 Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
 Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
 "The genome sequence of Schizosaccharomyces pombe.";
 Nature 415:871-880(2002).
 [3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-161; 636-871; 998-1098 AND
 1380-1547.
 PubMed=8769419; DOI=10.1083/jcb.134.4.949;
 Saitoh S., Takahashi K., Nabeshima K., Yamashita Y., Nakaseko Y.,
 Hirata A., Yanagida M.;
 "Aberrant mitosis in fission yeast mutants defective in fatty acid
 synthetase and acetyl CoA carboxylase.";
 J. Cell Biol. 134:949-961(1996).
 [4]
 INTERACTION WITH SAD1.
 PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
 Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
 "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
 membrane-bound components of the spindle pole body in fission yeast.";
 Mol. Genet. Genomics 270:449-461(2004).
 [5]
 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
 PubMed=16823372; DOI=10.1038/nbt1222;
 Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
 Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
 Yoshida M.;
 "ORFeome cloning and global analysis of protein localization in the
 fission yeast Schizosaccharomyces pombe.";
 Nat. Biotechnol. 24:841-847(2006).
 [6]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179 AND SER-1181, AND
 IDENTIFICATION BY MASS SPECTROMETRY.
 PubMed=18257517; DOI=10.1021/pr7006335;
 Wilson-Grady J.T., Villen J., Gygi S.P.;
 "Phosphoproteome analysis of fission yeast.";
 J. Proteome Res. 7:1088-1097(2008).
 -!- FUNCTION: Carries out three functions: biotin carboxyl carrier
     protein, biotin carboxylase and carboxyltransferase.
 -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
     + malonyl-CoA. {ECO:0000250|UniProtKB:Q00955}.
 -!- CATALYTIC ACTIVITY: ATP + [biotin carboxyl-carrier protein]-
     biotin-N(6)-L-lysine + hydrogencarbonate- = ADP + phosphate +
     [biotin carboxyl-carrier protein]-carboxybiotin-N(6)-L-lysine.
     {ECO:0000250|UniProtKB:Q5SWU9}.
 -!- COFACTOR:
     Name=biotin; Xref=ChEBI:CHEBI:57586;
       Evidence={ECO:0000250|UniProtKB:O00763};
 -!- COFACTOR:
     Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
     Note=Binds 2 manganese ions per subunit. {ECO:0000250};
 -!- ACTIVITY REGULATION: By phosphorylation. {ECO:0000250}.
 -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
     from acetyl-CoA: step 1/1.
 -!- SUBUNIT: Interacts with sad1. {ECO:0000269|PubMed:14655046}.
 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
 -!- SEQUENCE CAUTION:
     Sequence=BAA11916.1; Type=Frameshift; Positions=1511; Evidence={ECO:0000305};
     Sequence=BAA11917.1; Type=Frameshift; Positions=1005; Evidence={ECO:0000305};
 -----------------------------------------------------------------------
 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
 Distributed under the Creative Commons Attribution (CC BY 4.0) License
 -----------------------------------------------------------------------
 EMBL; D78169; BAA11238.1; -; Genomic_DNA.
 EMBL; CU329670; CAB16395.1; -; Genomic_DNA.
 EMBL; D83413; BAA11914.1; -; Genomic_DNA.
 EMBL; D83414; BAA11915.1; -; Genomic_DNA.
 EMBL; D83416; BAA11917.1; ALT_FRAME; Genomic_DNA.
 EMBL; D83415; BAA11916.1; ALT_FRAME; Genomic_DNA.
 PIR; T38906; T38906.
 PIR; T42531; T42531.
 RefSeq; NP_593271.1; NM_001018668.2.
 ProteinModelPortal; P78820; -.
 SMR; P78820; -.
 BioGrid; 279766; 3.
 IntAct; P78820; 1.
 STRING; 4896.SPAC56E4.04c.1; -.
 iPTMnet; P78820; -.
 MaxQB; P78820; -.
 PaxDb; P78820; -.
 PRIDE; P78820; -.
 EnsemblFungi; SPAC56E4.04c.1; SPAC56E4.04c.1:pep; SPAC56E4.04c.
 GeneID; 2543344; -.
 KEGG; spo:SPAC56E4.04c; -.
 EuPathDB; FungiDB:SPAC56E4.04c; -.
 PomBase; SPAC56E4.04c; cut6.
 HOGENOM; HOG000214115; -.
 InParanoid; P78820; -.
 KO; K11262; -.
 OMA; IPTLNRM; -.
 OrthoDB; EOG092C00TE; -.
 PhylomeDB; P78820; -.
 Reactome; R-SPO-163765; ChREBP activates metabolic gene expression.
 Reactome; R-SPO-196780; Biotin transport and metabolism.
 Reactome; R-SPO-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
 Reactome; R-SPO-75105; Fatty acyl-CoA biosynthesis.
 UniPathway; UPA00655; UER00711.
 PRO; PR:P78820; -.
 Proteomes; UP000002485; Chromosome I.
 GO; GO:0005737; C:cytoplasm; HDA:PomBase.
 GO; GO:0005829; C:cytosol; HDA:PomBase.
 GO; GO:0000329; C:fungal-type vacuole membrane; HDA:PomBase.
 GO; GO:0003989; F:acetyl-CoA carboxylase activity; ISO:PomBase.
 GO; GO:0005524; F:ATP binding; ISS:PomBase.
 GO; GO:0004075; F:biotin carboxylase activity; ISO:PomBase.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0006633; P:fatty acid biosynthetic process; NAS:PomBase.
 GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
 Gene3D; 3.30.1490.20; -; 1.
 InterPro; IPR034733; AcCoA_carboxyl.
 InterPro; IPR013537; AcCoA_COase_cen.
 InterPro; IPR011761; ATP-grasp.
 InterPro; IPR013815; ATP_grasp_subdomain_1.
 InterPro; IPR005481; BC-like_N.
 InterPro; IPR001882; Biotin_BS.
 InterPro; IPR011764; Biotin_carboxylation_dom.
 InterPro; IPR005482; Biotin_COase_C.
 InterPro; IPR000089; Biotin_lipoyl.
 InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
 InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
 InterPro; IPR011763; COA_CT_C.
 InterPro; IPR011762; COA_CT_N.
 InterPro; IPR016185; PreATP-grasp_dom_sf.
 InterPro; IPR011054; Rudment_hybrid_motif.
 InterPro; IPR011053; Single_hybrid_motif.
 Pfam; PF08326; ACC_central; 1.
 Pfam; PF02785; Biotin_carb_C; 1.
 Pfam; PF00289; Biotin_carb_N; 1.
 Pfam; PF00364; Biotin_lipoyl; 1.
 Pfam; PF01039; Carboxyl_trans; 1.
 Pfam; PF02786; CPSase_L_D2; 1.
 SMART; SM00878; Biotin_carb_C; 1.
 SUPFAM; SSF51230; SSF51230; 1.
 SUPFAM; SSF51246; SSF51246; 1.
 SUPFAM; SSF52096; SSF52096; 2.
 SUPFAM; SSF52440; SSF52440; 1.
 PROSITE; PS50975; ATP_GRASP; 1.
 PROSITE; PS50979; BC; 1.
 PROSITE; PS00188; BIOTIN; 1.
 PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
 PROSITE; PS50989; COA_CT_CTER; 1.
 PROSITE; PS50980; COA_CT_NTER; 1.
 PROSITE; PS00866; CPSASE_1; 1.
 PROSITE; PS00867; CPSASE_2; 1.
 1: Evidence at protein level;
 ATP-binding; Biotin; Complete proteome; Cytoplasm;
 Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
 Lipid biosynthesis; Lipid metabolism; Manganese; Metal-binding;
 Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
 Reference proteome.
 CHAIN         1   2280       Acetyl-CoA carboxylase.
                              /FTId=PRO_0000146769.
 DOMAIN       68    577       Biotin carboxylation.
 DOMAIN      226    418       ATP-grasp. {ECO:0000255|PROSITE-
                              ProRule:PRU00409}.
 DOMAIN      704    778       Biotinyl-binding. {ECO:0000255|PROSITE-
                              ProRule:PRU01066}.
 DOMAIN     1524   1863       CoA carboxyltransferase N-terminal.
                              {ECO:0000255|PROSITE-ProRule:PRU01136}.
 DOMAIN     1867   2181       CoA carboxyltransferase C-terminal.
                              {ECO:0000255|PROSITE-ProRule:PRU01137}.
 NP_BIND     266    271       ATP. {ECO:0000255|PROSITE-
                              ProRule:PRU00409}.
 REGION     1524   2181       Carboxyltransferase.
                              {ECO:0000255|PROSITE-ProRule:PRU01138}.
 ACT_SITE    393    393       {ECO:0000250}.
 METAL       375    375       Manganese 1. {ECO:0000250}.
 METAL       389    389       Manganese 1. {ECO:0000250}.
 METAL       389    389       Manganese 2. {ECO:0000250}.
 METAL       391    391       Manganese 2. {ECO:0000250}.
 BINDING    1772   1772       Coenzyme A. {ECO:0000250}.
 BINDING    2074   2074       Coenzyme A. {ECO:0000250}.
 BINDING    2076   2076       Coenzyme A. {ECO:0000250}.
 MOD_RES     745    745       N6-biotinyllysine. {ECO:0000250,
                              ECO:0000255|PROSITE-ProRule:PRU01066}.
 MOD_RES    1179   1179       Phosphoserine.
                              {ECO:0000269|PubMed:18257517}.
 MOD_RES    1181   1181       Phosphoserine.
                              {ECO:0000269|PubMed:18257517}.
 CONFLICT     14     42       LYAIKATISLPRLFYRRLRTMAPRVASHF -> RFIFIDVL
                              LISQLSISSFSFFILYFINHI (in Ref. 3;
                              BAA11914). {ECO:0000305}.
 CONFLICT    258    258       P -> S (in Ref. 1; BAA11238).
                              {ECO:0000305}.
 CONFLICT    339    340       IE -> L (in Ref. 1; BAA11238).
                              {ECO:0000305}.
 CONFLICT    512    512       A -> S (in Ref. 1; BAA11238).
                              {ECO:0000305}.
 CONFLICT    523    523       A -> T (in Ref. 1; BAA11238).
                              {ECO:0000305}.
 CONFLICT    636    639       DNTR -> YRIP (in Ref. 3; BAA11915).
                              {ECO:0000305}.
 CONFLICT   1017   1017       K -> N (in Ref. 3; BAA11917).
                              {ECO:0000305}.
 CONFLICT   1073   1073       R -> H (in Ref. 3; BAA11917).
                              {ECO:0000305}.
 CONFLICT   1098   1098       F -> L (in Ref. 3; BAA11917).
                              {ECO:0000305}.
 CONFLICT   1105   1105       V -> Y (in Ref. 1; BAA11238).
                              {ECO:0000305}.
 CONFLICT   1362   1362       R -> S (in Ref. 1; BAA11238).
                              {ECO:0000305}.
 CONFLICT   1427   1427       F -> Y (in Ref. 3; BAA11916).
                              {ECO:0000305}.
 CONFLICT   1444   1444       G -> E (in Ref. 1; BAA11238).
                              {ECO:0000305}.
 CONFLICT   1445   1445       F -> C (in Ref. 3; BAA11916).
                              {ECO:0000305}.
 CONFLICT   1449   1449       F -> L (in Ref. 3; BAA11916).
                              {ECO:0000305}.
 CONFLICT   1451   1451       R -> S (in Ref. 1; BAA11238).
                              {ECO:0000305}.
 CONFLICT   1465   1465       I -> F (in Ref. 3; BAA11916).
                              {ECO:0000305}.
 CONFLICT   1480   1480       V -> L (in Ref. 3; BAA11916).
                              {ECO:0000305}.
 CONFLICT   1485   1485       V -> L (in Ref. 3; BAA11916).
                              {ECO:0000305}.
 CONFLICT   1496   1496       A -> S (in Ref. 1; BAA11238).
                              {ECO:0000305}.
 SEQUENCE   2280 AA;  256843 MW;  8262C9A1A5C8E891 CRC64;
 MRQSVTSSSS CSKLYAIKAT ISLPRLFYRR LRTMAPRVAS HFLGGNSLDK APAGKVKDYI
 ASHGGHTVIT SILIANNGIA AVKEIRSIRK WAYETFNNER AIKFTVMATP DDLKVNADYI
 RMADQYVEVP GGSNNNNYAN VELIVDIAER MNVHAVWAGW GHASENPKLP EMLSASSKKI
 VFIGPPGSAM RSLGDKISST IVAQSARVPC MSWSGNELDQ VRIDEETNIV TVDDDVYQKA
 CIRSAEEGIA VAEKIGYPVM IKASEGGGGK GIRQVTSTEK FAQAFQQVLD ELPGSPVFVM
 KLAGQARHLE VQILADQYGN NISLFGRDCS VQRRHQKIIE EAPVTIAPAA TFHEMERAAV
 RLGELVGYAS AGTIEYLYEP ENDRFYFLEL NPRLQVEHPT TEMVSGVNLP AAQLQVAMGL
 PLSRIPHIRE LYGLPRDGDS EIDFFFQNPE SFKVQKVPTP KGHCVACRIT SEDPGEGFKP
 SSGMIKDLNF RSSSNVWGYF SVGTAGGIHE FADSQFGHIF SFAESRESSR KSMVVALKEL
 SIRGDFRTTV EYLVRLLETK EFSENEFTTG WLDRLIAQKV TSARPDKMLA VVCGALVRAH
 ATADTQYRAF KSYLERGQVP SREFLKNVYD IEFIYDNTRY RFTASRSSPG SYHLFLNGSR
 CTAGVRSLTD GGLLVLLNGH SYTVYYRDEV TGTRISIDNL SCMLEQENDP TQLRTPSPGK
 LVRFLVETGE HIKAGEAYAE VEVMKMIMPL VATEDGVVQL IKQPGASLDA GDILGILTLD
 DPSRVTHALP FDGQLPNWGE PQIAGNKPCQ RYHALLCILL DILKGYDNQI ILNSTYNEFV
 EVLRNHELPY SEWSAHYSAL VNRISPVLDK LFVSIIEKAR SRKAEFPAKQ LEVAIQTYCD
 GQNLATTQQL KVQIAPLLKI ISDYKDGLKV HEYNVIKGLL EEYYNVEKLF SGINKREEDV
 ILRLRDENKD DVDKVIALAL SHSRIGSKNN LLITILDLMK SEPSTFVSLY FNDILRKLTD
 LDSRVTSKVS LKARELLITC AMPSLNERFS QMEHILKSSV VESHYGDAKF SHRTPSLDIL
 KELIDSKYTV FDVLPAFFCH TDPWVSLAAL EVYVRRAYRA YSVLEINYHT EAGTPYVLTW
 RFQLHSSGAP GLGANSTNGS NFPASTTPSY ENSNRRLQSV SDLSWYVNKT DSEPFRFGTM
 IAAETFDELE NNLALAIDRL PLSRNYFNAG LTLDGNSSSA NDNTQELTNV VNVALTSTGD
 LDDSAIVSKL NQILSDFRDD LLEHNVRRVT IVGGRINKSA YPSYYTYRVS AEQKDGNLVH
 YNEDERIRHI EPALAFQLEL GRLSNFNIEP VFTDNHNIHV YRATAKNMDT DKRFFTRALV
 RPGRLRDEIP TAEYLISETH RLINDILDAL EVIGHEQTDL NHIFINFTPA FGLAPKQVEA
 ALGGFLERFG RRLWRLRVTA AEIRIICTDP STNTLFPLRV IISNVSGFVV NVEIYAEVKT
 ENNSWIFKSI GQPGSMHLRP ISTPYPTKEW LQPRRYKAQL MGTTFVYDFP ELFRRAFTDS
 WKKVPNGRSK VTIPQNMFEC KELVADEHGV LQEVNREPGT NSCGMVAWCI TVKTPEYPNG
 RKIIVVANDI TFQIGSFGPQ EDEYFYKVTQ LARQRGIPRI YLAANSGARI GVADEIVPLF
 NIAWVDPDSP EKGFDYIYLT PEAYERLQKE NPNILTTEEV VTETGELRHK ITTIIGSSEG
 LGVECLRGSG LIAGVTSRAY NDIFTCTLVT CRAVGIGAYL VRLGQRAVQI EGQPIILTGA
 PALNKVLGRE VYTSNLQLGG TQVMHRNGIS HLTSQDDFDG ISKIVNWISY IPDKRNNPVP
 ISPSSDTWDR DVEFYPSQNG YDPRWLIAGK EDEDSFLYGL FDKGSFQETL NGWAKTVVVG
 RARMGGIPTG VIAVETRTIE NTVPADPANP DSTEQVLMEA GQVWYPNSAF KTAQAINDFN
 HGEQLPLFIL ANWRGFSGGQ RDMFNEVLKY GSYIVDALAS YKQPVFVYIP PFSELRGGSW
 VVVDPTINED QMEMYADEES RAGVLEPEGM VSIKFRREKL LSLMRRCDHK YASLCNELKR
 DDLSADDLST IKVKLMEREQ KLMPIYQQIS IHFADLHDRV GRMVAKKVVR KPLKWTEARR
 FFYWRLRRRL NEHYALQKIT QLIPSLTIRE SREYLQKWYE EWCGKQDWDE SDKSVVCWIE
 EHNDDLSKRT QELKSTYYSE RLSKLLRSDR KGMIDSLAQV LTELDENEKK ELAGKLASVN

Related products :