mas

Functionⁱ

Catalyzes the elongation of long-chain fatty acyl-CoA with 3 or 4 methylmalonyl-CoA (not malonyl-CoA) as the elongating agent to form tri- or tetramethylated-branched fatty acids known as mycocerosyl lipids.

1 Publication

Catalytic activityⁱ

3
(R)-methylmalonyl-CoA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 9
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
long-chain fatty acyl-[mycocerosate synthase]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+ 6
NADPH
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
= 3
CO₂
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 3
CoA
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 3
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 6
NADP⁺
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
trimethylated-mycocerosoyl-[mycocerosate synthase]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.4
  "Fatty acid biosynthesis in Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin. Purification and characterization of a novel fatty acid synthase, mycocerosic acid synthase, which elongates n-fatty acyl-CoA with methylmalonyl-CoA."
  Rainwater D.L., Kolattukudy P.E.
  J. Biol. Chem. 260:616-623(1985) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.
EC:
2.3.1.111
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.4
  "Fatty acid biosynthesis in Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin. Purification and characterization of a novel fatty acid synthase, mycocerosic acid synthase, which elongates n-fatty acyl-CoA with methylmalonyl-CoA."
  Rainwater D.L., Kolattukudy P.E.
  J. Biol. Chem. 260:616-623(1985) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
3
(R)-methylmalonyl-CoA
zoom
+
9
H⁺
+
long-chain fatty acyl-[mycocerosate synthase]
O-(S-[long-chain fatty acyl]pantetheine-4'-phosphoryl)serine residue
zoom
+
6
NADPH
=
3
CO₂
+
3
CoA
+
3
H₂O
+
6
NADP⁺
zoom
+
trimethylated-mycocerosoyl-[mycocerosate synthase]
O-(S-[2R,4R,6R]-2,4,6-trimethyl-very-long-chain fatty acyl-pantetheine-4'-phosphoryl)serine residue
zoom
4
(R)-methylmalonyl-CoA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 12
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
long-chain fatty acyl-[mycocerosate synthase]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+ 8
NADPH
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
= 4
CO₂
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 4
CoA
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See the description of this molecule in ChEBI.
+ 4
H₂O
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See the description of this molecule in ChEBI.
+ 8
NADP⁺
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See the description of this molecule in ChEBI.
+
tetramethylated-mycocerosoyl-[mycocerosate synthase]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.4
  "Fatty acid biosynthesis in Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin. Purification and characterization of a novel fatty acid synthase, mycocerosic acid synthase, which elongates n-fatty acyl-CoA with methylmalonyl-CoA."
  Rainwater D.L., Kolattukudy P.E.
  J. Biol. Chem. 260:616-623(1985) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.
EC:
2.3.1.111
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.4
  "Fatty acid biosynthesis in Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin. Purification and characterization of a novel fatty acid synthase, mycocerosic acid synthase, which elongates n-fatty acyl-CoA with methylmalonyl-CoA."
  Rainwater D.L., Kolattukudy P.E.
  J. Biol. Chem. 260:616-623(1985) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
4
(R)-methylmalonyl-CoA
zoom
+
12
H⁺
+
long-chain fatty acyl-[mycocerosate synthase]
O-(S-[long-chain fatty acyl]pantetheine-4'-phosphoryl)serine residue
zoom
+
8
NADPH
=
4
CO₂
+
4
CoA
+
4
H₂O
+
8
NADP⁺
zoom
+
tetramethylated-mycocerosoyl-[mycocerosate synthase]
O-(S-[2R,4R,6R,8R]-2,4,6,8-tetramethyl-very-long-chain fatty acyl-pantetheine-4'-phosphoryl)serine residue
zoom

Cofactorⁱ

pantetheine 4'-phosphate1 PublicationNote: Binds 1 phosphopantetheine covalently.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	177	For beta-ketoacyl synthase activityPROSITE-ProRule annotation		1
Active siteⁱ	623	For acyltransferase activityPROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	1562 – 1579	NADP; for enoyl reductase activityAdd BLAST		18
Nucleotide bindingⁱ	1766 – 1781	NADP; for ketoreductase activityAdd BLAST		16

GO - Molecular functionⁱ

3-oxoacyl-[acyl-carrier-protein] synthase activity Source: InterPro
hydrolase activity Source: UniProtKB-KW
ligase activity Source: UniProtKB-KW
mycocerosate synthase activity Source: UniProtKB-EC
oxidoreductase activity Source: UniProtKB-KW
phosphopantetheine binding Source: InterPro

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

fatty acid biosynthetic process Source: UniProtKB-KW

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Ligase, Multifunctional enzyme, Oxidoreductase, Transferase
Biological process	Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
Ligand	NADP

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Mycocerosic acid synthase (EC:2.3.1.1111 Publication)
Gene namesⁱ	Name:mas Ordered Locus Names:BQ2027_MB2965C
Organismⁱ	Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifierⁱ	233413 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Actinobacteria › Actinomycetia › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium tuberculosis › Mycobacterium bovis
Proteomesⁱ	UP000001419 Componentⁱ: Chromosome

Keywords - Cellular componentⁱ

Cell membrane, Membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000180298	1 – 2111	Mycocerosic acid synthaseAdd BLAST		2111

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	2060	O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation		1

Keywords - PTMⁱ

Phosphopantetheine, Phosphoprotein

Interactionⁱ

Subunit structureⁱ

Homodimer whose monomers probably have a head to tail arrangement.

1 Publication

Structureⁱ

3D structure databases

SMRⁱ	Q02251
ModBaseⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	2025 – 2100	CarrierPROSITE-ProRule annotationAdd BLAST		76

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	1 – 430	Beta-ketoacyl synthaseAdd BLAST		430
Regionⁱ	533 – 852	AcyltransferaseAdd BLAST		320

Phylogenomic databases

OMAⁱ	PDFEWAI

OMAⁱ

PDFEWAI

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
InterProⁱ	View protein in InterPro IPR001227, Ac_transferase_dom_sf IPR036736, ACP-like_sf IPR014043, Acyl_transferase IPR016035, Acyl_Trfase/lysoPLipase IPR013149, ADH_C IPR013154, ADH_N 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 IPR016039, Thiolase-like
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00698, Acyl_transf_1, 1 hit PF08240, ADH_N, 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
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, 3 hits SSF52151, SSF52151, 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

Sequenceⁱ

Sequence statusⁱ: Complete.

Q02251-1 [UniParc]FASTA Add to basket

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        10         20         30         40         50
MESRVTPVAV IGMGCRLPGG INSPDKLWES LLRGDDLVTE IPPDRWDADD 
        60         70         80         90        100
YYDPEPGVPG RSVSRWGGFL DDVAGFDAEF FGISEREATS IDPQQRLLLE 
       110        120        130        140        150
TSWEAIEHAG LDPASLAGSS TAVFTGLTHE DYLVLTTTAG GLASPYVVTG 
       160        170        180        190        200
LNNSVASGRI AHTLGLHGPA MTFDTACSSG LMAVHLACRS LHDGEADLAL 
       210        220        230        240        250
AGGCAVLLEP HACVAASAQG MLSSTGRCHS FDADADGFVR SEGCAMVLLK 
       260        270        280        290        300
RLPDALRDGN RIFAVVRGTA TNQDGRTETL TMPSEDAQVA VYRAALAAAG 
       310        320        330        340        350
VQPETVGVVE AHGTGTPIGD PIEYRSLARV YGAGTPCALG SAKSNMGHST 
       360        370        380        390        400
ASAGTVGLIK AILSLRHGVV PPLLHFNRLP DELSDVETGL FVPQAVTPWP 
       410        420        430        440        450
NGNDHTPKRV AVSSFGMSGT NVHAIVEEAP AEASAPESSP GDAEVGPRLF 
       460        470        480        490        500
MLSSTSSDAL RQTARQLATW VEEHQDCVAA SDLAYTLARG RAHRPVRTAV 
       510        520        530        540        550
VAANLPELVE GLREVADGDA LYDAAVGHGD RGPVWVFSGQ GSQWAAMGTQ 
       560        570        580        590        600
LLASEPVFAA TIAKLEPVIA AESGFSVTEA ITAQQTVTGI DKVQPAVFAV 
       610        620        630        640        650
QVALAATMEQ TYGVRPGAVV GHSMGESAAA VVAGALSLED AARVICRRSK 
       660        670        680        690        700
LMTRIAGAGA MGSVELPAKQ VNSELMARGI DDVVVSVVAS PQSTVIGGTS 
       710        720        730        740        750
DTVRDLIARW EQRDVMAREV AVDVASHSPQ VDPILDDLAA ALADIAPMTP 
       760        770        780        790        800
KVPYYSATLF DPREQPVCDG AYWVDNLRNT VQFAAAVQAA MEDGYRVFAE 
       810        820        830        840        850
LSPHPLLTHA VEQTGRSLDM SVAALAGMRR EQPLPHGLRG LLTELHRAGA 
       860        870        880        890        900
ALDYSALYPA GRLVDAPLPA WTHARLFIDD DGQEQRAQGA CTITVHPLLG 
       910        920        930        940        950
SHVRLTEEPE RHVWQGDVGT SVLSWLSDHQ VHNVAALPGA AYCEMALAAA 
       960        970        980        990       1000
AEVFGEAAEV RDITFEQMLL LDEQTPIDAV ASIDAPGVVN FTVETNRDGE 
      1010       1020       1030       1040       1050
TTRHATAALR AAEDDCPPPG YDITALLQAH PHAVNGTAMR ESFAERGVTL 
      1060       1070       1080       1090       1100
GAAFGGLTTA HTAEAGAATV LAEVALPASI RFQQGAYRIH PALLDACFQS 
      1110       1120       1130       1140       1150
VGAGVQAGTA TGGLLLPLGV RSLRAYGPTR NARYCYTRLT KAFNDGTRGG 
      1160       1170       1180       1190       1200
EADLDVLDEH GTVLLAVRGL RMGTGTSERD ERDRLVSERL LTLGWQQRAL 
      1210       1220       1230       1240       1250
PEVGDGEAGS WLLIDTSNAV DTPDMLASTL TDALKSHGPQ GTECASLSWS 
      1260       1270       1280       1290       1300
VQDTPPNDQA GLEKLGSQLR GRDGVVIVYG PRVGDPDEHS LLAGREQVRH 
      1310       1320       1330       1340       1350
LVRITRELAE FEGELPRLFV VTRQAQIVKP HDSGERANLE QAGLRGLLRV 
      1360       1370       1380       1390       1400
ISSEHPMLRT TLIDVDEHTD VERVAQQLLS GSEEDETAWR NGDWYVARLT 
      1410       1420       1430       1440       1450
PSPLGHEERR TAVLDPDHDG MRVQVRRPGD LQTLEFVASD RVPPGPGQIE 
      1460       1470       1480       1490       1500
VAVSMSSINF ADVLIAFGRF PIIDDREPQL GMDFVGVVTA VGEGVTGHQV 
      1510       1520       1530       1540       1550
GDRVGGFSEG GCWRTFLTCD ANLAVTLPPG LTDEQAITAA TAHATAWYGL 
      1560       1570       1580       1590       1600
NDLAQIKAGD KVLIHSATGG VGQAAISIAR AKGAEIFATA GNPAKRAMLR 
      1610       1620       1630       1640       1650
DMGVEHVYDS RSVEFAEQIR RDTDGYGVDI VLNSLTGAAQ RAGLELLAFG 
      1660       1670       1680       1690       1700
GRFVEIGKAD VYGNTRLGLF PFRRGLTFYY LDLALMSVTQ PDRVRELLAT 
      1710       1720       1730       1740       1750
VFKLTADGVL TAPQCTHYPL AEAADAIRAM SNAEHTGKLV LDVPRSGRRS 
      1760       1770       1780       1790       1800
VAVTPEQAPL YRRDGSYIIT GGLGGLGLFF ASKLAAAGCG RIVLTARSQP 
      1810       1820       1830       1840       1850
NPKARQTIEG LRAAGADIVV ECGNIAEPDT ADRLVSAATA TGLPLRGVLH 
      1860       1870       1880       1890       1900
SAAVVEDATL TNITDELIDR DWSPKVFGSW NLHRATLGQP LDWFCLFSSG 
      1910       1920       1930       1940       1950
AALLGSPGQG AYAAANSWVD VFAHWRRAQG LPVSAIAWGA WGEVGRATFL 
      1960       1970       1980       1990       2000
AEGGEIMITP EEGAYAFETL VRHDRAYSGY IPILGAPWLA DLVRRSPWGE 
      2010       2020       2030       2040       2050
MFASTGQRSR GPSKFRMELL SLPQDEWAGR LRRLLVEQAS VILRRTIDAD 
      2060       2070       2080       2090       2100
RSFIEYGLDS LGMLEMRTHV ETETGIRLTP KVIATNNTAR ALAQYLADTL 
      2110 
AEEQAAAPAA S

Length:2,111

Mass (Da):224,396

Last modified:July 11, 2003 - v2

Checksum:ⁱ5CE2B96E083660FC

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	196	A → R in AAA25369 (PubMed:1527058).Curated	1
Sequence conflictⁱ	492	A → R in AAA25369 (PubMed:1527058).Curated	1
Sequence conflictⁱ	800 – 801	EL → DV in AAA25369 (PubMed:1527058).Curated	2
Sequence conflictⁱ	1063 – 1150	AEAGA…GTRGG → PRREPRRCWPRSRCPRRSGS SRAPTESTRRCWTLVSSRSA RASSRYGHWWPAVAVGCAQP ACLRAYPQCPLLLHAVDQGL QRRDPRW in AAA25369 (PubMed:1527058).CuratedAdd BLAST	88
Sequence conflictⁱ	1648	A → P in AAA25369 (PubMed:1527058).Curated	1
Sequence conflictⁱ	1758	A → R in AAA25369 (PubMed:1527058).Curated	1
Sequence conflictⁱ	1926	R → P in AAA25369 (PubMed:1527058).Curated	1
Sequence conflictⁱ	2087	N → K in AAA25369 (PubMed:1527058).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M95808 Genomic DNA Translation: AAA25369.1 LT708304 Genomic DNA Translation: SIU01586.1
PIRⁱ	B44110
NCBI Reference Sequences More...RefSeqⁱ	NP_856610.1, NC_002945.3 WP_010950802.1, NC_002945.4

Genome annotation databases

EnsemblBacteriaⁱ	SIU01586; SIU01586; BQ2027_MB2965C
PATRICⁱ	fig\|233413.5.peg.3254

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q02251	PROBABLE MULTIFUNCTIONAL MYCOCEROSIC ACID SYNTHASE MEMBRANE-ASSOCIATED MAS		MYCBO		2111	UniRef100_Q02251
Probable multifunctional mycocerosic acid synthase membrane-associated mas		MYCBP		2111
Multifunctional mycocerosic acid synthase membrane-associated MAS		Mycobacterium tuberculosis variant bovis BCG str. Korea 1168P		2111
Multifunctional mycocerosic acid synthase		Mycobacterium tuberculosis variant bovis BCG		155
Multifunctional mycocerosic acid synthase membrane-associated MAS		MYCTX		887
+13

Protein	Similar proteins		Species	Score	Length	Source
Q02251	PROBABLE MULTIFUNCTIONAL MYCOCEROSIC ACID SYNTHASE MEMBRANE-ASSOCIATED MAS		MYCBO		2111	UniRef90_Q02251
Probable multifunctional mycocerosic acid synthase membrane-associated mas		MYCBP		2111
Multifunctional mycocerosic acid synthase membrane-associated MAS		Mycobacterium tuberculosis variant bovis BCG str. Korea 1168P		2111
Multifunctional mycocerosic acid synthase		Mycobacterium tuberculosis variant bovis BCG		155
Multifunctional mycocerosic acid synthase membrane-associated MAS		MYCTX		887
+324

Protein	Similar proteins		Species	Score	Length	Source
Q02251	Mycolipanoate synthase		MYCTU		2085	UniRef50_A0A089QRB9
Polyketide beta-ketoacyl synthase		Mycobacterium tuberculosis NCGM2209		2085
Mycocerosic acid synthase		MYCTX		2085
Type I polyketide synthase		Mycobacterium orygis		2085
Polyketide beta-ketoacyl synthase Pks3		MYCTA		2085
+1235

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M95808 Genomic DNA Translation: AAA25369.1 LT708304 Genomic DNA Translation: SIU01586.1
PIRⁱ	B44110
RefSeqⁱ	NP_856610.1, NC_002945.3 WP_010950802.1, NC_002945.4

3D structure databases

SMRⁱ	Q02251
ModBaseⁱ	Search...

Genome annotation databases

EnsemblBacteriaⁱ	SIU01586; SIU01586; BQ2027_MB2965C
PATRICⁱ	fig\|233413.5.peg.3254

Phylogenomic databases

OMAⁱ	PDFEWAI

OMAⁱ

PDFEWAI

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
InterProⁱ	View protein in InterPro IPR001227, Ac_transferase_dom_sf IPR036736, ACP-like_sf IPR014043, Acyl_transferase IPR016035, Acyl_Trfase/lysoPLipase IPR013149, ADH_C IPR013154, ADH_N 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 IPR016039, Thiolase-like
Pfamⁱ	View protein in Pfam PF00698, Acyl_transf_1, 1 hit PF08240, ADH_N, 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
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, 3 hits SSF52151, SSF52151, 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	MCAS_MYCBO
Accessionⁱ	Q02251Primary (citable) accession number: Q02251 Secondary accession number(s): A0A1R3Y3F3, X2BLY1
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
	Last sequence update:	July 11, 2003
	Last modified:	February 23, 2022
	This is version 158 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Direct protein sequencing

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q02251 (MCAS_MYCBO)

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Mycocerosic acid synthase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Plasma Membrane

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ