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P78820 (ACAC_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-CoA carboxylase

Short name=ACC
EC=6.4.1.2
Alternative name(s):
Cell untimely torn protein 6

Including the following 1 domains:

  1. Biotin carboxylase
    EC=6.3.4.14
Gene names
Name:cut6
ORF Names:SPAC56E4.04c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length2280 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.

Catalytic activity

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

Cofactor

Biotin By similarity.

Binds 2 manganese ions per subunit By similarity.

Enzyme regulation

By phosphorylation By similarity.

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.

Subunit structure

Interacts with sad1. Ref.4

Subcellular location

Cytoplasm Ref.5.

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Contains 1 carboxyltransferase domain.

Sequence caution

The sequence BAA11916.1 differs from that shown. Reason: Frameshift at position 1511.

The sequence BAA11917.1 differs from that shown. Reason: Frameshift at position 1005.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22802280Acetyl-CoA carboxylase
PRO_0000146769

Regions

Domain68 – 577510Biotin carboxylation
Domain226 – 418193ATP-grasp
Domain711 – 77767Biotinyl-binding
Domain1644 – 2141498Carboxyltransferase
Nucleotide binding266 – 2716ATP By similarity

Sites

Active site3931 By similarity
Metal binding3751Manganese 1 By similarity
Metal binding3891Manganese 1 By similarity
Metal binding3891Manganese 2 By similarity
Metal binding3911Manganese 2 By similarity
Binding site17721Coenzyme A By similarity
Binding site20741Coenzyme A By similarity
Binding site20761Coenzyme A By similarity

Amino acid modifications

Modified residue7451N6-biotinyllysine By similarity
Modified residue11791Phosphoserine Ref.6
Modified residue11811Phosphoserine Ref.6

Experimental info

Sequence conflict14 – 4229LYAIK…VASHF → RFIFIDVLLISQLSISSFSF FILYFINHI in BAA11914. Ref.3
Sequence conflict2581P → S in BAA11238. Ref.1
Sequence conflict339 – 3402IE → L in BAA11238. Ref.1
Sequence conflict5121A → S in BAA11238. Ref.1
Sequence conflict5231A → T in BAA11238. Ref.1
Sequence conflict636 – 6394DNTR → YRIP in BAA11915. Ref.3
Sequence conflict10171K → N in BAA11917. Ref.3
Sequence conflict10731R → H in BAA11917. Ref.3
Sequence conflict10981F → L in BAA11917. Ref.3
Sequence conflict11051V → Y in BAA11238. Ref.1
Sequence conflict13621R → S in BAA11238. Ref.1
Sequence conflict14271F → Y in BAA11916. Ref.3
Sequence conflict14441G → E in BAA11238. Ref.1
Sequence conflict14451F → C in BAA11916. Ref.3
Sequence conflict14491F → L in BAA11916. Ref.3
Sequence conflict14511R → S in BAA11238. Ref.1
Sequence conflict14651I → F in BAA11916. Ref.3
Sequence conflict14801V → L in BAA11916. Ref.3
Sequence conflict14851V → L in BAA11916. Ref.3
Sequence conflict14961A → S in BAA11238. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P78820 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 8262C9A1A5C8E891

FASTA2,280256,843
        10         20         30         40         50         60 
MRQSVTSSSS CSKLYAIKAT ISLPRLFYRR LRTMAPRVAS HFLGGNSLDK APAGKVKDYI 

        70         80         90        100        110        120 
ASHGGHTVIT SILIANNGIA AVKEIRSIRK WAYETFNNER AIKFTVMATP DDLKVNADYI 

       130        140        150        160        170        180 
RMADQYVEVP GGSNNNNYAN VELIVDIAER MNVHAVWAGW GHASENPKLP EMLSASSKKI 

       190        200        210        220        230        240 
VFIGPPGSAM RSLGDKISST IVAQSARVPC MSWSGNELDQ VRIDEETNIV TVDDDVYQKA 

       250        260        270        280        290        300 
CIRSAEEGIA VAEKIGYPVM IKASEGGGGK GIRQVTSTEK FAQAFQQVLD ELPGSPVFVM 

       310        320        330        340        350        360 
KLAGQARHLE VQILADQYGN NISLFGRDCS VQRRHQKIIE EAPVTIAPAA TFHEMERAAV 

       370        380        390        400        410        420 
RLGELVGYAS AGTIEYLYEP ENDRFYFLEL NPRLQVEHPT TEMVSGVNLP AAQLQVAMGL 

       430        440        450        460        470        480 
PLSRIPHIRE LYGLPRDGDS EIDFFFQNPE SFKVQKVPTP KGHCVACRIT SEDPGEGFKP 

       490        500        510        520        530        540 
SSGMIKDLNF RSSSNVWGYF SVGTAGGIHE FADSQFGHIF SFAESRESSR KSMVVALKEL 

       550        560        570        580        590        600 
SIRGDFRTTV EYLVRLLETK EFSENEFTTG WLDRLIAQKV TSARPDKMLA VVCGALVRAH 

       610        620        630        640        650        660 
ATADTQYRAF KSYLERGQVP SREFLKNVYD IEFIYDNTRY RFTASRSSPG SYHLFLNGSR 

       670        680        690        700        710        720 
CTAGVRSLTD GGLLVLLNGH SYTVYYRDEV TGTRISIDNL SCMLEQENDP TQLRTPSPGK 

       730        740        750        760        770        780 
LVRFLVETGE HIKAGEAYAE VEVMKMIMPL VATEDGVVQL IKQPGASLDA GDILGILTLD 

       790        800        810        820        830        840 
DPSRVTHALP FDGQLPNWGE PQIAGNKPCQ RYHALLCILL DILKGYDNQI ILNSTYNEFV 

       850        860        870        880        890        900 
EVLRNHELPY SEWSAHYSAL VNRISPVLDK LFVSIIEKAR SRKAEFPAKQ LEVAIQTYCD 

       910        920        930        940        950        960 
GQNLATTQQL KVQIAPLLKI ISDYKDGLKV HEYNVIKGLL EEYYNVEKLF SGINKREEDV 

       970        980        990       1000       1010       1020 
ILRLRDENKD DVDKVIALAL SHSRIGSKNN LLITILDLMK SEPSTFVSLY FNDILRKLTD 

      1030       1040       1050       1060       1070       1080 
LDSRVTSKVS LKARELLITC AMPSLNERFS QMEHILKSSV VESHYGDAKF SHRTPSLDIL 

      1090       1100       1110       1120       1130       1140 
KELIDSKYTV FDVLPAFFCH TDPWVSLAAL EVYVRRAYRA YSVLEINYHT EAGTPYVLTW 

      1150       1160       1170       1180       1190       1200 
RFQLHSSGAP GLGANSTNGS NFPASTTPSY ENSNRRLQSV SDLSWYVNKT DSEPFRFGTM 

      1210       1220       1230       1240       1250       1260 
IAAETFDELE NNLALAIDRL PLSRNYFNAG LTLDGNSSSA NDNTQELTNV VNVALTSTGD 

      1270       1280       1290       1300       1310       1320 
LDDSAIVSKL NQILSDFRDD LLEHNVRRVT IVGGRINKSA YPSYYTYRVS AEQKDGNLVH 

      1330       1340       1350       1360       1370       1380 
YNEDERIRHI EPALAFQLEL GRLSNFNIEP VFTDNHNIHV YRATAKNMDT DKRFFTRALV 

      1390       1400       1410       1420       1430       1440 
RPGRLRDEIP TAEYLISETH RLINDILDAL EVIGHEQTDL NHIFINFTPA FGLAPKQVEA 

      1450       1460       1470       1480       1490       1500 
ALGGFLERFG RRLWRLRVTA AEIRIICTDP STNTLFPLRV IISNVSGFVV NVEIYAEVKT 

      1510       1520       1530       1540       1550       1560 
ENNSWIFKSI GQPGSMHLRP ISTPYPTKEW LQPRRYKAQL MGTTFVYDFP ELFRRAFTDS 

      1570       1580       1590       1600       1610       1620 
WKKVPNGRSK VTIPQNMFEC KELVADEHGV LQEVNREPGT NSCGMVAWCI TVKTPEYPNG 

      1630       1640       1650       1660       1670       1680 
RKIIVVANDI TFQIGSFGPQ EDEYFYKVTQ LARQRGIPRI YLAANSGARI GVADEIVPLF 

      1690       1700       1710       1720       1730       1740 
NIAWVDPDSP EKGFDYIYLT PEAYERLQKE NPNILTTEEV VTETGELRHK ITTIIGSSEG 

      1750       1760       1770       1780       1790       1800 
LGVECLRGSG LIAGVTSRAY NDIFTCTLVT CRAVGIGAYL VRLGQRAVQI EGQPIILTGA 

      1810       1820       1830       1840       1850       1860 
PALNKVLGRE VYTSNLQLGG TQVMHRNGIS HLTSQDDFDG ISKIVNWISY IPDKRNNPVP 

      1870       1880       1890       1900       1910       1920 
ISPSSDTWDR DVEFYPSQNG YDPRWLIAGK EDEDSFLYGL FDKGSFQETL NGWAKTVVVG 

      1930       1940       1950       1960       1970       1980 
RARMGGIPTG VIAVETRTIE NTVPADPANP DSTEQVLMEA GQVWYPNSAF KTAQAINDFN 

      1990       2000       2010       2020       2030       2040 
HGEQLPLFIL ANWRGFSGGQ RDMFNEVLKY GSYIVDALAS YKQPVFVYIP PFSELRGGSW 

      2050       2060       2070       2080       2090       2100 
VVVDPTINED QMEMYADEES RAGVLEPEGM VSIKFRREKL LSLMRRCDHK YASLCNELKR 

      2110       2120       2130       2140       2150       2160 
DDLSADDLST IKVKLMEREQ KLMPIYQQIS IHFADLHDRV GRMVAKKVVR KPLKWTEARR 

      2170       2180       2190       2200       2210       2220 
FFYWRLRRRL NEHYALQKIT QLIPSLTIRE SREYLQKWYE EWCGKQDWDE SDKSVVCWIE 

      2230       2240       2250       2260       2270       2280 
EHNDDLSKRT QELKSTYYSE RLSKLLRSDR KGMIDSLAQV LTELDENEKK ELAGKLASVN 

« Hide

References

« Hide 'large scale' references
[1]"Biotin-dependent enzymes in Schizosaccharomyces pombe: cloning and nucleotide sequences of acetyl-CoA carboxylase and pyruvate carboxylase."
Saito A., Kazuta Y., Toh H., Kondo H., Tanabe T.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 972 / HM123.
[2]"The genome sequence of Schizosaccharomyces pombe."
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. expand/collapse author list , 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.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Aberrant mitosis in fission yeast mutants defective in fatty acid synthetase and acetyl CoA carboxylase."
Saitoh S., Takahashi K., Nabeshima K., Yamashita Y., Nakaseko Y., Hirata A., Yanagida M.
J. Cell Biol. 134:949-961(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 14-161; 636-871; 998-1098 AND 1380-1547.
[4]"Two-hybrid search for proteins that interact with Sad1 and Kms1, two membrane-bound components of the spindle pole body in fission yeast."
Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.
Mol. Genet. Genomics 270:449-461(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SAD1.
[5]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179 AND SER-1181, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D78169 Genomic DNA. Translation: BAA11238.1.
CU329670 Genomic DNA. Translation: CAB16395.1.
D83413 Genomic DNA. Translation: BAA11914.1.
D83414 Genomic DNA. Translation: BAA11915.1.
D83416 Genomic DNA. Translation: BAA11917.1. Frameshift.
D83415 Genomic DNA. Translation: BAA11916.1. Frameshift.
PIRT38906.
T42531.
RefSeqNP_593271.1. NM_001018668.2.

3D structure databases

ProteinModelPortalP78820.
SMRP78820. Positions 41-559, 699-793, 1520-2261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279766. 6 interactions.
IntActP78820. 1 interaction.
MINTMINT-4691347.
STRING4896.SPAC56E4.04c-1.

Proteomic databases

PaxDbP78820.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC56E4.04c.1; SPAC56E4.04c.1:pep; SPAC56E4.04c.
GeneID2543344.
KEGGspo:SPAC56E4.04c.

Organism-specific databases

PomBaseSPAC56E4.04c.

Phylogenomic databases

eggNOGCOG0511.
HOGENOMHOG000214115.
KOK11262.
OMASNNGIAH.
OrthoDBEOG74J9H5.
PhylomeDBP78820.

Enzyme and pathway databases

UniPathwayUPA00655; UER00711.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProIPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
IPR000022. Carboxyl_trans.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF08326. ACC_central. 1 hit.
PF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804359.

Entry information

Entry nameACAC_SCHPO
AccessionPrimary (citable) accession number: P78820
Secondary accession number(s): O94557 expand/collapse secondary AC list , Q09447, Q09576, Q09616, Q09667
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 11, 2001
Last modified: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways