ID   LCF4_YEAST              Reviewed;         694 AA.
AC   P47912; Q05743;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase 4;
DE            EC=6.2.1.3;
DE   AltName: Full=Long-chain acyl-CoA synthetase 4;
DE   AltName: Full=Fatty acid activator 4;
GN   Name=FAA4; OrderedLocusNames=YMR246W; ORFNames=YM9408.08;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   MEDLINE=95050946; PubMed=7962057; DOI=10.1083/jcb.127.3.751;
RA   Johnson D.R., Knoll L.J., Levin D.E., Gordon J.I.;
RT   "Saccharomyces cerevisiae contains four fatty acid activation (FAA)
RT   genes: an assessment of their role in regulating protein N-
RT   myristoylation and cellular lipid metabolism.";
RL   J. Cell Biol. 127:751-762(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313268; PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
RA   Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
RA   Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   XIII.";
RL   Nature 387:90-93(1997).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Esterification, concomitant with transport, of exogenous
CC       long-chain fatty acids into metabolically active CoA thioesters
CC       for subsequent degradation or incorporation into phospholipids.
CC       Contributes, with FAA1, to the activation of imported myristate.
CC   -!- CATALYTIC ACTIVITY: ATP + a long-chain carboxylic acid + CoA = AMP
CC       + diphosphate + an acyl-CoA.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- MISCELLANEOUS: Present with 31200 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z48744; CAA88635.1; -; Genomic_DNA.
DR   EMBL; Z48756; CAA88656.1; -; Genomic_DNA.
DR   PIR; S56060; S56060.
DR   RefSeq; NP_013974.1; -.
DR   HSSP; P08659; 1LCI.
DR   DIP; DIP:4361N; -.
DR   IntAct; P47912; 27.
DR   PeptideAtlas; P47912; -.
DR   PRIDE; P47912; -.
DR   Ensembl; YMR246W; Saccharomyces cerevisiae.
DR   GeneID; 855288; -.
DR   GenomeReviews; Z71257_GR; YMR246W.
DR   KEGG; sce:YMR246W; -.
DR   NMPDR; fig|4932.3.peg.5029; -.
DR   CYGD; YMR246w; -.
DR   SGD; S000004860; FAA4.
DR   HOGENOM; P47912; -.
DR   OMA; P47912; VMVGVAA.
DR   BRENDA; 6.2.1.3; 250.
DR   NextBio; 978932; -.
DR   ArrayExpress; P47912; -.
DR   GermOnline; YMR246W; Saccharomyces cerevisiae.
DR   GO; GO:0005811; C:lipid particle; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004467; F:long-chain-fatty-acid-CoA ligase activity; IDA:SGD.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IGI:SGD.
DR   GO; GO:0006499; P:N-terminal protein myristoylation; IGI:SGD.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Fatty acid metabolism; Ligase;
KW   Lipid metabolism; Magnesium; Nucleotide-binding.
FT   CHAIN         1    694       Long-chain-fatty-acid--CoA ligase 4.
FT                                /FTId=PRO_0000193122.
FT   CONFLICT    552    552       N -> G (in Ref. 1; CAA88635).
FT   CONFLICT    631    631       V -> G (in Ref. 1; CAA88635).
SQ   SEQUENCE   694 AA;  77267 MW;  CF6524949C96D24D CRC64;
     MTEQYSVAVG EAANEHETAP RRNIRVKDQP LIRPINSSAS TLYEFALECF TKGGKRDGMA
     WRDIIDIHET KKTIVKRVDG KDKPIEKTWL YYELTPYITM TYEEMICVMH DIGRGLIKIG
     VKPNGENKFH IFASTSHKWM KTFLGCMSQG IPVVTAYDTL GESGLIHSMV ETDSVAIFTD
     NQLLSKLAVP LKTAKNVKFV IHNEPIDPSD KRQNGKLYKA AKDAVDKIKE VRPDIKIYSF
     DEIIEIGKKA KDEVELHFPK PEDPACIMYT SGSTGTPKGV VLTHYNIVAG IGGVGHNVIG
     WIGPTDRIIA FLPLAHIFEL TFEFEAFYWN GILGYANVKT LTPTSTRNCQ GDLMEFKPTV
     MVGVAAVWET VRKGILAKIN ELPGWSQTLF WTVYALKERN IPCSGLLSGL IFKRIREATG
     GNLRFILNGG SAISIDAQKF LSNLLCPMLI GYGLTEGVAN ACVLEPEHFD YGIAGDLVGT
     ITAKLVDVED LGYFAKNNQG ELLFKGAPIC SEYYKNPEET AAAFTDDGWF RTGDIAEWTP
     KGQVKIIDRK KNLVKTLNGE YIALEKLESI YRSNPYVQNI CVYADENKVK PVGIVVPNLG
     HLSKLAIELG IMVPGEDVES YIHEKKLQDA VCKDMLSTAK SQGLNGIELL CGIVFFEEEW
     TPENGLVTSA QKLKRRDILA AVKPDVERVY KENT
//