| General information | | DisProt: | DP00557 | | Name: | Acetyl-CoA carboxylase | | Synonym(s): | ACAC_YEAST
ACC
EC 6.4.1.2
Biotin carboxylase [domain 1]
EC=6.3.4.14
| | First appeared in release: | Release 4.0 (06/23/2008) | | UniProt: | Q00955 | | UniGene: | | | SwissProt: | ACAC_YEAST | | TrEMBL: | | | NCBI (GI): | 1705966 | | Source organism: | Saccharomyces cerevisiae (Baker's yeast) | | Sequence length: | 2233 | | Percent disordered: | 4% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MSEESLFESS PQKMEYEITN YSERHTELPG HFIGLNTVDK LEESPLRDFV KSHGGHTVIS - 60
KILIANNGIA AVKEIRSVRK WAYETFGDDR TVQFVAMATP EDLEANAEYI RMADQYIEVP - 120
GGTNNNNYAN VDLIVDIAER ADVDAVWAGW GHASENPLLP EKLSQSKRKV IFIGPPGNAM - 180
RSLGDKISST IVAQSAKVPC IPWSGTGVDT VHVDEKTGLV SVDDDIYQKG CCTSPEDGLQ - 240
KAKRIGFPVM IKASEGGGGK GIRQVEREED FIALYHQAAN EIPGSPIFIM KLAGRARHLE - 300
VQLLADQYGT NISLFGRDCS VQRRHQKIIE EAPVTIAKAE TFHEMEKAAV RLGKLVGYVS - 360
AGTVEYLYSH DDGKFYFLEL NPRLQVEHPT TEMVSGVNLP AAQLQIAMGI PMHRISDIRT - 420
LYGMNPHSAS EIDFEFKTQD ATKKQRRPIP KGHCTACRIT SEDPNDGFKP SGGTLHELNF - 480
RSSSNVWGYF SVGNNGNIHS FSDSQFGHIF AFGENRQASR KHMVVALKEL SIRGDFRTTV - 540
EYLIKLLETE DFEDNTITTG WLDDLITHKM TAEKPDPTLA VICGAATKAF LASEEARHKY - 600
IESLQKGQVL SKDLLQTMFP VDFIHEGKRY KFTVAKSGND RYTLFINGSK CDIILRQLSD - 660
GGLLIAIGGK SHTIYWKEEV AATRLSVDSM TTLLEVENDP TQLRTPSPGK LVKFLVENGE - 720
HIIKGQPYAE IEVMKMQMPL VSQENGIVQL LKQPGSTIVA GDIMAIMTLD DPSKVKHALP - 780
FEGMLPDFGS PVIEGTKPAY KFKSLVSTLE NILKGYDNQV IMNASLQQLI EVLRNPKLPY - 840
SEWKLHISAL HSRLPAKLDE QMEELVARSL RRGAVFPARQ LSKLIDMAVK NPEYNPDKLL - 900
GAVVEPLADI AHKYSNGLEA HEHSIFVHFL EEYYEVEKLF NGPNVREENI ILKLRDENPK - 960
DLDKVALTVL SHSKVSAKNN LILAILKHYQ PLCKLSSKVS AIFSTPLQHI VELESKATAK - 1020
VALQAREILI QGALPSVKER TEQIEHILKS SVVKVAYGSS NPKRSEPDLN ILKDLIDSNY - 1080
VVFDVLLQFL THQDPVVTAA AAQVYIRRAY RAYTIGDIRV HEGVTVPIVE WKFQLPSAAF - 1140
STFPTVKSKM GMNRAVSVSD LSYVANSQSS PLREGILMAV DHLDDVDEIL SQSLEVIPRH - 1200
QSSSNGPAPD RSGSSASLSN VANVCVASTE GFESEEEILV RLREILDLNK QELINASIRR - 1260
ITFMFGFKDG SYPKYYTFNG PNYNENETIR HIEPALAFQL ELGRLSNFNI KPIFTDNRNI - 1320
HVYEAVSKTS PLDKRFFTRG IIRTGHIRDD ISIQEYLTSE ANRLMSDILD NLEVTDTSNS - 1380
DLNHIFINFI AVFDISPEDV EAAFGGFLER FGKRLLRLRV SSAEIRIIIK DPQTGAPVPL - 1440
RALINNVSGY VIKTEMYTEV KNAKGEWVFK SLGKPGSMHL RPIATPYPVK EWLQPKRYKA - 1500
HLMGTTYVYD FPELFRQASS SQWKNFSADV KLTDDFFISN ELIEDENGEL TEVEREPGAN - 1560
AIGMVAFKIT VKTPEYPRGR QFVVVANDIT FKIGSFGPQE DEFFNKVTEY ARKRGIPRIY - 1620
LAANSGARIG MAEEIVPLFQ VAWNDAANPD KGFQYLYLTS EGMETLKKFD KENSVLTERT - 1680
VINGEERFVI KTIIGSEDGL GVECLRGSGL IAGATSRAYH DIFTITLVTC RSVGIGAYLV - 1740
RLGQRAIQVE GQPIILTGAP AINKMLGREV YTSNLQLGGT QIMYNNGVSH LTAVDDLAGV - 1800
EKIVEWMSYV PAKRNMPVPI LETKDTWDRP VDFTPTNDET YDVRWMIEGR ETESGFEYGL - 1860
FDKGSFFETL SGWAKGVVVG RARLGGIPLG VIGVETRTVE NLIPADPANP NSAETLIQEP - 1920
GQVWHPNSAF KTAQAINDFN NGEQLPMMIL ANWRGFSGGQ RDMFNEVLKY GSFIVDALVD - 1980
YKQPIIIYIP PTGELRGGSW VVVDPTINAD QMEMYADVNA RAGVLEPQGM VGIKFRREKL - 2040
LDTMNRLDDK YRELRSQLSN KSLAPEVHQQ ISKQLADRER ELLPIYGQIS LQFADLHDRS - 2100
SRMVAKGVIS KELEWTEARR FFFWRLRRRL NEEYLIKRLS HQVGEASRLE KIARIRSWYP - 2160
ASVDHEDDRQ VATWIEENYK TLDDKLKGLK LESFAQDLAK KIRSDHDNAI DGLSEVIKML - 2220
STDDKEKLLK TLK
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| Functional narrative |
Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. The protein is required for the synthesis and oxidation of long-chain fatty acids. The protein is a dimer composed of two domains: nitrogen and carbon monomers, which contribute equal portions to the protein. The active site of the protein is located at the interface of the dimer between the small beta sheets of the beta-beta-alpha superhelix. In X-ray crystallography an electron density was determined for the adenine base, but the remaining coenzyme lacked any electron density suggesting it to be disordered in the binding site. Furthermore, the 50 residues of the N-terminus and 30 residues of the C-terminus were indicated to be disordered according to its crystal structure.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | N-Terminus | | Location: | 1429 - 1494 | | Length: | 66 | | Region sequence: |
IKDPQTGAPVPLRALINNVSGYVIKTEMYTEVKNAKGEWVFKSLGKPGSMHLRPIATPYP
VKEWLQ | | Modification type: | Native
| | PDB: | 1OD2:A | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Modification site
Molecular assembly
| | Functional subclasses: | Fatty acylation (myristolation and palmitoylation)
Substrate/ligand binding
| Detection methods:
| References:
- Zhang H, Tweel B, Li J, Tong L. "Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase in complex with CP-640186." Structure. 2004; 12(9): 1683-91. PubMed: 15341732
| Comments:
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| Region 2 | | Type: | Disordered | | Name: | C-Terminus | | Location: | 2204 - 2233 | | Length: | 30 | | Region sequence: |
SDHDNAIDGLSEVIKMLSTDDKEKLLKTLK | | Modification type: | Native
| | PDB: | 1OD2:A | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Modification site
Molecular assembly
| | Functional subclasses: | Fatty acylation (myristolation and palmitoylation)
Substrate/ligand binding
| Detection methods:
| References:
There are no documents referencing this region. | Comments:
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| Comments |
In order to determine crystal structure of protein a His tag was added to the C-terminus.
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| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
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