P9WQE7

PR
Gene name
ppsA (Rv2931, MTCY338.20)
Protein name
Phenolphthiocerol/phthiocerol polyketide synthase subunit A
Names
(Phenol)carboxyphthiodiolenone synthase subunit A, Beta-ketoacyl-acyl-carrier-protein synthase I, Phthiocerol synthesis polyketide synthase type I PpsA
Species
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
KEGG Pathway
mtu:Rv2931
EC number
2.3.1.292: Transferring groups other than amino-acyl groups
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1810-1876 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P9WQE7

Entry ID Method Resolution Chain Position Source
AF-P9WQE7-F1 Predicted AlphaFoldDB

No variants for P9WQE7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P9WQE7

No associated diseases with P9WQE7

13 regional properties for P9WQE7

Type Name Position InterPro Accession
ptm Phosphopantetheine attachment site 1791 - 1806 IPR006162
domain Phosphopantetheine binding ACP domain 9 - 83 IPR009081-1
domain Phosphopantetheine binding ACP domain 1759 - 1836 IPR009081-2
domain Polyketide synthase, ketoreductase domain 1491 - 1683 IPR013968
domain Beta-ketoacyl synthase, N-terminal 102 - 351 IPR014030
domain Beta-ketoacyl synthase, C-terminal 359 - 477 IPR014031
domain Acyl transferase 632 - 949 IPR014043
active_site Beta-ketoacyl synthase, active site 264 - 280 IPR018201
domain Polyketide synthase, phosphopantetheine-binding domain 12 - 83 IPR020806-1
domain Polyketide synthase, phosphopantetheine-binding domain 1765 - 1836 IPR020806-2
domain Polyketide synthase, dehydratase domain 991 - 1261 IPR020807
domain Polyketide synthase, beta-ketoacyl synthase domain 101 - 529 IPR020841
domain Polyketide synthase, C-terminal extension 480 - 584 IPR032821

Functions

Description
EC Number 2.3.1.292 Transferring groups other than amino-acyl groups
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
peptidoglycan-based cell wall A protective structure outside the cytoplasmic membrane composed of peptidoglycan (also known as murein), a molecule made up of a glycan (sugar) backbone of repetitively alternating N-acetylglucosamine and N-acetylmuramic acid with short, attached, cross-linked peptide chains containing unusual amino acids. An example of this component is found in Escherichia coli.
polyketide synthase complex A protein complex that carries out enzymatic reactions involved in the biosynthesis of polyketides, any of a diverse group of natural products synthesized via linear poly-beta-ketones.

5 GO annotations of molecular function

Name Definition
3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Catalysis of the reaction: (3R)-3-hydroxyacyl-
3-oxoacyl-[acyl-carrier-protein] synthase activity Catalysis of the reaction: acyl-
acyl carrier activity Binding an acyl group and presenting it for processing or offloading to a cognate enzyme. Covalently binds the acyl group via a phosphopantetheine prosthetic group and mediates protein-protein interactions with the enzyme conferring specificity. The acyl carrier protein (ACP) presents substrates to enzymes involved in fatty acid biosynthesis or in polyketide secondary metabolite biosynthesis.
fatty acid synthase activity Catalysis of the reaction: acetyl-CoA + n malonyl-CoA + 2n NADPH + 2n H+ = long-chain fatty acid + n+1 CoA + n CO2 + 2n NADP+.
phosphopantetheine binding Binding to phosphopantetheine, the vitamin pantetheine 4'-(dihydrogen phosphate).

4 GO annotations of biological process

Name Definition
DIM/DIP cell wall layer assembly The aggregation, arrangement and bonding together of a set of components, including (phenyl)phthiocerol, phthiodiolone, phthiotriol dimycocerosate and diphthioceranate, to form the DIM/DIP layer of the Actinobacterium-type cell wall.
fatty acid biosynthetic process The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
phenolic phthiocerol biosynthetic process The chemical reactions and pathways resulting in the formation of phenolic phthiocerol, a phthiocerol derivative having a 4-hydroxyphenyl substituent at the 29-position.
phthiocerol biosynthetic process The chemical reactions and pathways resulting in the formation of phthiocerol, a lipid-based 1,3-glycol consisting of (3S,4R)-3-methoxy-4-methylnonacosane having (9R)- and (11S)-hydroxy substituents.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTGSISGEAD LRHWLIDYLV TNIGCTPDEV DPDLSLADLG VSSRDAVVLS GELSELLGRT
70 80 90 100 110 120
VSPIDFWEHP TINALAAYLA APEPSPDSDA AVKRGARNSL DEPIAVVGMG CRFPGGISCP
130 140 150 160 170 180
EALWDFLCER RSSISQVPPQ RWQPFEGGPP EVAAALARTT RWGSFLPDID AFDAEFFEIS
190 200 210 220 230 240
PSEADKMDPQ QRLLLEVAWE ALEHAGIPPG TLRRSATGVF AGACLSEYGA MASADLSQVD
250 260 270 280 290 300
GWSNSGGAMS IIANRLSYFL DLRGPSVAVD TACSSSLVAI HLACQSLRTQ DCHLAIAAGV
310 320 330 340 350 360
NLLLSPAVFR GFDQVGALSP TGQCRAFDAT ADGFVRGEGA GVVVLKRLTD AQRDGDRVLA
370 380 390 400 410 420
VICGSAVNQD GRSNGLMAPN PAAQMAVLRA AYTNAGMQPS EVDYVEAHGT GTLLGDPIEA
430 440 450 460 470 480
RALGTVLGRG RPEDSPLLIG SVKTNLGHTE AAAGIAGFIK TVLAVQHGQI PPNQHFETAN
490 500 510 520 530 540
PHIPFTDLRM KVVDTQTEWP ATGHPRRAGV SSFGFGGTNA HVVIEQGQEV RPAPGQGLSP
550 560 570 580 590 600
AVSTLVVAGK TMQRVSATAG MLADWMEGPG ADVALADVAH TLNHHRSRQP KFGTVVARDR
610 620 630 640 650 660
TQAIAGLRAL AAGQHAPGVV NPADGSPGPG TVFVYSGRGS QWAGMGRQLL ADEPAFAAAV
670 680 690 700 710 720
AELEPVFVEQ AGFSLHDVLA NGEELVGIEQ IQLGLIGMQL ALTELWCSYG VRPDLVIGHS
730 740 750 760 770 780
MGEVAAAVVA GALTPAEGLR VTATRSRLMA PLSGQGGMAL LELDAPTTEA LIADFPQVTL
790 800 810 820 830 840
GIYNSPRQTV IAGPTEQIDE LIARVRAQNR FASRVNIEVA PHNPAMDALQ PAMRSELADL
850 860 870 880 890 900
TPRTPTIGII STTYADLHTQ PVFDAEHWAT NMRNPVRFQQ AIASAGSGAD GAYHTFIEIS
910 920 930 940 950 960
AHPLLTQAII DTLHSAQPGA RYTSLGTLQR DTDDVVTFRT NLNKAHTIHP PHTPHPPEPH
970 980 990 1000 1010 1020
PPIPTTPWQH TRHWITTKYP AGSVGSAPRA GTLLGQHTTV ATVSASPPSH LWQARLAPDA
1030 1040 1050 1060 1070 1080
KPYQGGHRFH QVEVVPASVV LHTILSAATE LGYSALSEVR FEQPIFADRP RLIQVVADNR
1090 1100 1110 1120 1130 1140
AISLASSPAA GTPSDRWTRH VTAQLSSSPS DSASSLNEHH RANGQPPERA HRDLIPDLAE
1150 1160 1170 1180 1190 1200
LLAMRGIDGL PFSWTVASWT QHSSNLTVAI DLPEALPEGS TGPLLDAAVH LAALSDVADS
1210 1220 1230 1240 1250 1260
RLYVPASIEQ ISLGDVVTGP RSSVTLNRTA HDDDGITVDV TVAAHGEVPS LSMRSLRYRA
1270 1280 1290 1300 1310 1320
LDFGLDVGRA QPPASTGPVE AYCDATNFVH TIDWQPQTVP DATHPGAEQV THPGPVAIIG
1330 1340 1350 1360 1370 1380
DDGAALCETL EGAGYQPAVM SDGVSQARYV VYVADSDPAG ADETDVDFAV RICTEITGLV
1390 1400 1410 1420 1430 1440
RTLAERDADK PAALWILTRG VHESVAPSAL RQSFLWGLAG VIAAEHPELW GGLVDLAIND
1450 1460 1470 1480 1490 1500
DLGEFGPALA ELLAKPSKSI LVRRDGVVLA PALAPVRGEP ARKSLQCRPD AAYLITGGLG
1510 1520 1530 1540 1550 1560
ALGLLMADWL ADRGAHRLVL TGRTPLPPRR DWQLDTLDTE LRRRIDAIRA LEMRGVTVEA
1570 1580 1590 1600 1610 1620
VAADVGCRED VQALLAARDR DGAAPIRGII HAAGITNDQL VTSMTGDAVR QVMWPKIGGS
1630 1640 1650 1660 1670 1680
QVLHDAFPPG SVDFFYLTAS AAGIFGIPGQ GSYAAANSYL DALARARRQQ GCHTMSLDWV
1690 1700 1710 1720 1730 1740
AWRGLGLAAD AQLVSEELAR MGSRDITPSE AFTAWEFVDG YDVAQAVVVP MPAPAGADGS
1750 1760 1770 1780 1790 1800
GANAYLLPAR NWSVMAATEV RSELEQGLRR IIAAELRVPE KELDTDRPFA ELGLNSLMAM
1810 1820 1830 1840 1850 1860
AIRREAEQFV GIELSATMLF NHPTVKSLAS YLAKRVAPHD VSQDNQISAL SSSAGSVLDS
1870
LFDRIESAPP EAERSV