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Acetyl-CoA carboxylase (ACC) (EC 6.4.1.2) (Cell untimely torn protein 6) [Includes: Biotin carboxylase (EC 6.3.4.14)]

 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.
05-JUL-2017, entry version 161.
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] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein]. {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};
-!- ENZYME 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};
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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.
MINT; MINT-4691347; -.
STRING; 4896.SPAC56E4.04c.1; -.
iPTMnet; P78820; -.
MaxQB; 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; FTPPCQR; -.
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; IDA:PomBase.
GO; GO:0005829; C:cytosol; IDA:PomBase.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA: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.
InterPro; IPR011763; COA_CT_C.
InterPro; IPR011762; COA_CT_N.
InterPro; IPR016185; PreATP-grasp_dom.
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


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