UniProtKB - P12276 (FAS_CHICK)
Fatty acid synthase
FASN
Functioni
Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain.
4 PublicationsCatalytic activityi
- acetyl-CoA + 2n H+ + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + n CO2 + (n+1) CoA + 2n NADP+4 PublicationsEC:2.3.1.854 PublicationsThis reaction proceeds in the forward4 Publications direction.
- EC:2.3.1.382 PublicationsThis reaction proceeds in the forward2 Publications direction.
- EC:2.3.1.392 PublicationsThis reaction proceeds in the forward2 Publications direction.
- EC:2.3.1.411 PublicationThis reaction proceeds in the forward1 Publication direction.
- EC:1.1.1.1003 PublicationsThis reaction proceeds in the backward3 Publications direction.
- EC:4.2.1.592 PublicationsThis reaction proceeds in the forward2 Publications direction.
- EC:1.3.1.391 PublicationThis reaction proceeds in the backward1 Publication direction.
- EC:3.1.2.143 PublicationsThis reaction proceeds in the forward3 Publications direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forward3 Publications direction.
- This reaction proceeds in the forward2 Publications direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- EC:3.1.2.14By similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forward1 Publication direction.
Activity regulationi
: fatty acid biosynthesis Pathwayi
This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.4 PublicationsView all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 161 | For beta-ketoacyl synthase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 580 | For acyl/malonyl transferase activityPROSITE-ProRule annotation | 1 | |
Binding sitei | 670 | Acyl-CoABy similarity | 1 | |
Binding sitei | 772 | Acyl-CoABy similarity | 1 | |
Active sitei | 878 | For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2309 | For thioesterase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2482 | For thioesterase activityPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1675 – 1692 | NADP; for enoyl reductase activityAdd BLAST | 18 | |
Nucleotide bindingi | 1889 – 1904 | NADP; for ketoreductase activityAdd BLAST | 16 |
GO - Molecular functioni
- (3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
- [acyl-carrier-protein] S-acetyltransferase activity Source: UniProtKB-EC
- [acyl-carrier-protein] S-malonyltransferase activity Source: UniProtKB-EC
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
- 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
- 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
- 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB-EC
- 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: UniProtKB-EC
- enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity Source: UniProtKB-EC
- fatty acid synthase activity Source: GO_Central
- myristoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
- oleoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
- palmitoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
- phosphopantetheine binding Source: InterPro
- single-stranded DNA binding Source: AgBase
GO - Biological processi
- fatty acid biosynthetic process Source: GO_Central
- lactate metabolic process Source: AgBase
- positive regulation of appetite Source: AgBase
Keywordsi
Molecular function | Hydrolase, Lyase, Multifunctional enzyme, Oxidoreductase, Transferase |
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Ligand | NAD, NADP, Pyridoxal phosphate |
Enzyme and pathway databases
SABIO-RKi | P12276 |
UniPathwayi | UPA00094 |
Protein family/group databases
ESTHERi | chick-fas, Thioesterase |
Names & Taxonomyi
Protein namesi | Recommended name: Fatty acid synthase (EC:2.3.1.854 Publications)Including the following 7 domains: [Acyl-carrier-protein] S-acetyltransferase (EC:2.3.1.382 Publications) [Acyl-carrier-protein] S-malonyltransferase (EC:2.3.1.392 Publications) 3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.411 Publication) 3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.1003 Publications) 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.592 Publications) Enoyl-[acyl-carrier-protein] reductase (EC:1.3.1.391 Publication) Acyl-[acyl-carrier-protein] hydrolase (EC:3.1.2.143 Publications) |
Gene namesi | Name:FASN Synonyms:FAS |
Organismi | Gallus gallus (Chicken) |
Taxonomic identifieri | 9031 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archelosauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galloanserae › Galliformes › Phasianidae › Phasianinae › Gallus |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000180273 | 2 – 2512 | Fatty acid synthaseAdd BLAST | 2511 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylglutamate1 Publication | 1 | |
Modified residuei | 1475 | S-nitrosocysteineBy similarity | 1 | |
Modified residuei | 1708 | N6-(pyridoxal phosphate)lysineBy similarity | 1 | |
Modified residuei | 2093 | S-nitrosocysteineBy similarity | 1 | |
Modified residuei | 2158 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Phosphopantetheine, Phosphoprotein, S-nitrosylationProteomic databases
PaxDbi | P12276 |
PTM databases
iPTMneti | P12276 |
Interactioni
Subunit structurei
Homodimer which is arranged in a head to tail fashion.
By similarityProtein-protein interaction databases
STRINGi | 9031.ENSGALP00000004327 |
Chemistry databases
BindingDBi | P12276 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2120 – 2200 | CarrierPROSITE-ProRule annotationAdd BLAST | 81 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – ?412 | Beta-ketoacyl synthaseAdd BLAST | 411 | |
Regioni | 427 – 815 | Acyl and malonyl transferasesAdd BLAST | 389 | |
Regioni | 646 – 647 | Acyl-CoA bindingBy similarity | 2 | |
Regioni | 1638 – 1866 | Enoyl reductaseAdd BLAST | 229 | |
Regioni | 1867 – 2119 | Beta-ketoacyl reductaseAdd BLAST | 253 | |
Regioni | 2209 – 2511 | ThioesteraseAdd BLAST | 303 |
Phylogenomic databases
eggNOGi | KOG1202, Eukaryota KOG2335, Eukaryota |
InParanoidi | P12276 |
OrthoDBi | 993446at2759 |
PhylomeDBi | P12276 |
Family and domain databases
Gene3Di | 1.10.1200.10, 1 hit 3.10.129.110, 1 hit 3.40.366.10, 1 hit 3.40.47.10, 1 hit 3.40.50.1820, 2 hits |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR001227, Ac_transferase_dom_sf IPR036736, ACP-like_sf IPR014043, Acyl_transferase IPR016035, Acyl_Trfase/lysoPLipase IPR013149, ADH_C IPR011032, GroES-like_sf IPR018201, Ketoacyl_synth_AS IPR014031, Ketoacyl_synth_C IPR014030, Ketoacyl_synth_N IPR016036, Malonyl_transacylase_ACP-bd IPR036291, NAD(P)-bd_dom_sf IPR032821, PKS_assoc IPR020841, PKS_Beta-ketoAc_synthase_dom IPR020807, PKS_dehydratase IPR042104, PKS_dehydratase_sf IPR020843, PKS_ER IPR013968, PKS_KR IPR020806, PKS_PP-bd IPR009081, PP-bd_ACP IPR006162, Ppantetheine_attach_site IPR029063, SAM-dependent_MTases IPR001031, Thioesterase IPR016039, Thiolase-like |
Pfami | View protein in Pfam PF00698, Acyl_transf_1, 1 hit PF00107, ADH_zinc_N, 1 hit PF16197, KAsynt_C_assoc, 1 hit PF00109, ketoacyl-synt, 1 hit PF02801, Ketoacyl-synt_C, 1 hit PF08659, KR, 1 hit PF00550, PP-binding, 1 hit PF14765, PS-DH, 1 hit PF00975, Thioesterase, 1 hit |
SMARTi | View protein in SMART SM00827, PKS_AT, 1 hit SM00826, PKS_DH, 1 hit SM00829, PKS_ER, 1 hit SM00825, PKS_KS, 1 hit SM00823, PKS_PP, 1 hit |
SUPFAMi | SSF47336, SSF47336, 1 hit SSF50129, SSF50129, 1 hit SSF51735, SSF51735, 2 hits SSF52151, SSF52151, 1 hit SSF53335, SSF53335, 1 hit SSF53474, SSF53474, 1 hit SSF53901, SSF53901, 1 hit SSF55048, SSF55048, 1 hit |
PROSITEi | View protein in PROSITE PS00606, B_KETOACYL_SYNTHASE, 1 hit PS50075, CARRIER, 1 hit PS00012, PHOSPHOPANTETHEINE, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MEDVVIAGIA GKLPESENLQ EFWENLLNGV DMVTEDDRRW KPGIYGLPKR
60 70 80 90 100
NGKLKDIKKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI LDGGINPTAL
110 120 130 140 150
RGTDTGVWVG ASGSEALEAL SQDPEELLGY SMTGCQRAML ANRISYFYDF
160 170 180 190 200
TGPSLTIDTA CSSSLMALEN AYKAIRHGQC SAALVGGVNI LLKPNTSVQF
210 220 230 240 250
MKLGMLSPDG ACKAFDVSGN GYCRSEAVVV VLLTKKSMAK RVYATIVNAG
260 270 280 290 300
SNTDGFKEQG VTFPSGEMQQ QLVGSLYREC GIKPGDVEYV EAHGTGTKVG
310 320 330 340 350
DPQEVNGIVN VFCQCEREPL LIGSTKSNMG HPEPASGLAA LAKVILSLEH
360 370 380 390 400
GLWAPNLHFN DPNPDIPALH DGSLKVVCKP TPVKGGLVSI NSFGFGGSNA
410 420 430 440 450
HVILRPNEKK CQPQETCNLP RLVQVCGRTQ EAVEILIEES RKHGGCSPFL
460 470 480 490 500
SLLSDISAVP VSSMPYRGYT LVGTESDITE IQQVQASGRP LWYICSGMGT
510 520 530 540 550
QWKGMGLSLM KLDLFRQSIL RSDEALKSTG LKVSDLLLNA DENTFDDTVH
560 570 580 590 600
AFVGLAAIQI AQIDVLKAAG LQPDGILGHS VGELACGYAD NSLSHEEAVL
610 620 630 640 650
AAYWRGRCVK EAKLPPGGMA AVGLTWEECK QRCPPNVVPA CHNSEDTVTV
660 670 680 690 700
SGPLDSVSEF VTKLKKDGVF AKEVRRAGVA FHSYYMASIA PALLSALKKV
710 720 730 740 750
IPHPKPRSAR WISTSIPESQ WQSDLARNSS AEYHVNNLVN PVLFHEGLKH
760 770 780 790 800
IPENAVVVEI APHALLQAIL RRTLKPTCTI LPLMKKDHKN NLEFFLTQTG
810 820 830 840 850
KIHLTGINVL GNNLFPPVEY PVPVGTPLIS PYIKWDHSQD WDVPKAEDFP
860 870 880 890 900
SGSKGSASAS VYNIDVSPDS PDHYLVGHCI DGRVLYPATG YLVLAWRTLA
910 920 930 940 950
RSLGMVMEQT AVMFEEVTIH QATILPKKGS TQLEVRIMPA SHSFEVSGNG
960 970 980 990 1000
NLAVSGKISL LENDALKNFH NQLADFQSQA NVTAKSGLLM EDVYQELHLR
1010 1020 1030 1040 1050
GYNYGPTFQG VLECNSEGSA GKILWNGNWV TFLDTLLHLI VLAETGRSLR
1060 1070 1080 1090 1100
LPTRIRSVYI DPVLHQEQVY QYQDNVEAFD VVVDRCLDSL KAGGVQINGL
1110 1120 1130 1140 1150
HASVAPRRQQ ERISPTLEKF SFVPYIESDC LSSSTQLHAY LEHCKGLIQK
1160 1170 1180 1190 1200
LQAKMALHGV KLVIHGLETK GAAAGSPPAQ KGLQHILTEI CRLELNGNPH
1210 1220 1230 1240 1250
SELEQIVTQE KMHLQDDPLL NGLLDSSELK TCLDVAKENT TSHRMKIVEA
1260 1270 1280 1290 1300
LAGSGRLFSR VQSILNTQPL LQLDYIATDC TPETLSDNET ELHDAGISFS
1310 1320 1330 1340 1350
QWDPSSLPSG NLTNADLAVC NCSTSVLGNT AEIISNLAAA VKEGGFVLLH
1360 1370 1380 1390 1400
TLLKEETLGE IVSFLTSPDL QQKHSFLSQA QWEELFSKAS LNLVAMKRSF
1410 1420 1430 1440 1450
FGSVIFLCRR QSPAKAPILL PVDDTHYKWV DSLKEILADS SEQPLWLTAT
1460 1470 1480 1490 1500
NCGNSGILGM VNCLRLEAEG HRIRCVFVSN LSPSSTVPAT SLSSLEMQKI
1510 1520 1530 1540 1550
IERDLVMNVY RDGKWGSFRH LPLQQAQPQE LTECAYVNVL TRGDLSSLRW
1560 1570 1580 1590 1600
IVSPLRHFQT TNPNVQLCKV YYASLNFWDI MLATGKLSPD AIPGNWTLQQ
1610 1620 1630 1640 1650
CMLGMEFSGR DLAGRRVMGL LPAKGLATVV DCDKRFLWEV PENWTLEEAA
1660 1670 1680 1690 1700
SVPVVYATAY YALVVRGGMK KGESVLIHSG SGGVGQAAIA IALSMGCRVF
1710 1720 1730 1740 1750
ATVGSAEKRE YLQARFPQLD ANSFASSRNT TFQQHILRVT NGKGVSLVLN
1760 1770 1780 1790 1800
SLAEEKLQAS LRCLAQHGRF LEIGKFDLSN NSQLGMALFL KNVAFHGILL
1810 1820 1830 1840 1850
DSIFEEGNQE WEVVSELLTK GIKDGVVKPL RTTVFGKEEV EAAFRFMAQG
1860 1870 1880 1890 1900
KHIGKVMIKI QEEEKQYPLR SEPVKLSAIS RTSCPPTKSY IITGGLGGFG
1910 1920 1930 1940 1950
LELAQWLIER GAQKLVLTSR SGIRTGYQAK CVREWKALGI QVLVSTSDVG
1960 1970 1980 1990 2000
TLEGTQLLIE EALKLGPVGG IFNLAVVLKD AMIENQTPEL FWEVNKPKYS
2010 2020 2030 2040 2050
GTLHLDWVTR KKCPDLDYFV VFSSVSCGRG NAGQSNYGFA NSAMERICEQ
2060 2070 2080 2090 2100
RHHDGLPGLA VQWGAIGDVG ILKAMGNREV VIGGTVLQQI SSCLEVLDMF
2110 2120 2130 2140 2150
LNQPHPVMSS FVLAEKVSVK SEGGSQRDLV EAVAHILGVR DVSSLNAESS
2160 2170 2180 2190 2200
LADLGLDSLM GVEVRQTLER DYDIVMTMRE IRLLTINKLR ELSSKTGTAE
2210 2220 2230 2240 2250
ELKPSQVLKT GPGEPPKLDL NNLLVNPEGP TITRLNEVQS TERPLFLVHP
2260 2270 2280 2290 2300
IEGSIAVFYT LASKLHMPCY GLQCTKAAPL DSIQSLASYY IDCMKQIQPE
2310 2320 2330 2340 2350
GPYRIAGYSF GACVAFEMCS QLQAQQNASH ALNSLFLFDG SHSFVAAYTQ
2360 2370 2380 2390 2400
SYRAKLTQGN EAALETEALC AFVQQFTGIE YNKLLEILLP LEDLEARVNA
2410 2420 2430 2440 2450
AADLITQIHK NINREALSFA AASFYHKLKA ADKYIPESKY HGNVTLMRAK
2460 2470 2480 2490 2500
THNEYEEGLG GDYRLSEVCD GKVSVHIIEG DHRTLLEGDG VESIIGIIHG
2510
SLAEPRVSVR EG
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 78 – 79 | QL → PV in AAA48767 (PubMed:2734291).Curated | 2 | |
Sequence conflicti | 117 | L → A in AAA48767 (PubMed:2734291).Curated | 1 | |
Sequence conflicti | 676 | R → S in AAA48767 (PubMed:2734291).Curated | 1 | |
Sequence conflicti | 1170 | K → N in AAA48767 (PubMed:2734291).Curated | 1 | |
Sequence conflicti | 1179 | A → T in AAA48767 (PubMed:2734291).Curated | 1 | |
Sequence conflicti | 1192 | R → H in AAA48767 (PubMed:2734291).Curated | 1 | |
Sequence conflicti | 1199 | P → L in AAA48767 (PubMed:2734291).Curated | 1 | |
Sequence conflicti | 1287 – 1288 | DN → ND in AAA48767 (PubMed:2734291).Curated | 2 | |
Sequence conflicti | 1373 | K → E in AAA48767 (PubMed:2734291).Curated | 1 | |
Sequence conflicti | 1534 | C → Y in AAA48767 (PubMed:2734291).Curated | 1 | |
Sequence conflicti | 1578 | W → R in AAA48767 (PubMed:2734291).Curated | 1 | |
Sequence conflicti | 1686 – 1697 | QAAIA…LSMGC → ASSHCHRLEHGLA in AAA48767 (PubMed:2734291).CuratedAdd BLAST | 12 | |
Sequence conflicti | 1733 | Q → E in AAA48767 (PubMed:2734291).Curated | 1 | |
Sequence conflicti | 1746 | S → N in AAA48767 (PubMed:2734291).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_000149 | 2349 | T → TQCFSFSLF in isoform 1. Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03860 mRNA Translation: AAA48767.1 J04485 mRNA Translation: AAB46389.1 J02839 Genomic DNA Translation: AAA82106.1 Frameshift. |
PIRi | S57248, XYCHFA |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03860 mRNA Translation: AAA48767.1 J04485 mRNA Translation: AAB46389.1 J02839 Genomic DNA Translation: AAA82106.1 Frameshift. |
PIRi | S57248, XYCHFA |
3D structure databases
SMRi | P12276 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9031.ENSGALP00000004327 |
Chemistry databases
BindingDBi | P12276 |
ChEMBLi | CHEMBL1795136 |
Protein family/group databases
ESTHERi | chick-fas, Thioesterase |
PTM databases
iPTMneti | P12276 |
Proteomic databases
PaxDbi | P12276 |
Phylogenomic databases
eggNOGi | KOG1202, Eukaryota KOG2335, Eukaryota |
InParanoidi | P12276 |
OrthoDBi | 993446at2759 |
PhylomeDBi | P12276 |
Enzyme and pathway databases
UniPathwayi | UPA00094 |
SABIO-RKi | P12276 |
Miscellaneous databases
PROi | PR:P12276 |
Family and domain databases
Gene3Di | 1.10.1200.10, 1 hit 3.10.129.110, 1 hit 3.40.366.10, 1 hit 3.40.47.10, 1 hit 3.40.50.1820, 2 hits |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR001227, Ac_transferase_dom_sf IPR036736, ACP-like_sf IPR014043, Acyl_transferase IPR016035, Acyl_Trfase/lysoPLipase IPR013149, ADH_C IPR011032, GroES-like_sf IPR018201, Ketoacyl_synth_AS IPR014031, Ketoacyl_synth_C IPR014030, Ketoacyl_synth_N IPR016036, Malonyl_transacylase_ACP-bd IPR036291, NAD(P)-bd_dom_sf IPR032821, PKS_assoc IPR020841, PKS_Beta-ketoAc_synthase_dom IPR020807, PKS_dehydratase IPR042104, PKS_dehydratase_sf IPR020843, PKS_ER IPR013968, PKS_KR IPR020806, PKS_PP-bd IPR009081, PP-bd_ACP IPR006162, Ppantetheine_attach_site IPR029063, SAM-dependent_MTases IPR001031, Thioesterase IPR016039, Thiolase-like |
Pfami | View protein in Pfam PF00698, Acyl_transf_1, 1 hit PF00107, ADH_zinc_N, 1 hit PF16197, KAsynt_C_assoc, 1 hit PF00109, ketoacyl-synt, 1 hit PF02801, Ketoacyl-synt_C, 1 hit PF08659, KR, 1 hit PF00550, PP-binding, 1 hit PF14765, PS-DH, 1 hit PF00975, Thioesterase, 1 hit |
SMARTi | View protein in SMART SM00827, PKS_AT, 1 hit SM00826, PKS_DH, 1 hit SM00829, PKS_ER, 1 hit SM00825, PKS_KS, 1 hit SM00823, PKS_PP, 1 hit |
SUPFAMi | SSF47336, SSF47336, 1 hit SSF50129, SSF50129, 1 hit SSF51735, SSF51735, 2 hits SSF52151, SSF52151, 1 hit SSF53335, SSF53335, 1 hit SSF53474, SSF53474, 1 hit SSF53901, SSF53901, 1 hit SSF55048, SSF55048, 1 hit |
PROSITEi | View protein in PROSITE PS00606, B_KETOACYL_SYNTHASE, 1 hit PS50075, CARRIER, 1 hit PS00012, PHOSPHOPANTETHEINE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | FAS_CHICK | |
Accessioni | P12276Primary (citable) accession number: P12276 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1989 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 182 of the entry and version 5 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways