D1ZA70

PR
Gene name
SMAC_02366
Protein name
Pentafunctional AROM polypeptide
Names
Species
Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell)
KEGG Pathway
smp:SMAC_02366
EC number
1.1.1.25: With NAD(+) or NADP(+) as acceptor
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

808-882 (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 D1ZA70

Entry ID Method Resolution Chain Position Source
AF-D1ZA70-F1 Predicted AlphaFoldDB

No variants for D1ZA70

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for D1ZA70

No associated diseases with D1ZA70

9 regional properties for D1ZA70

Type Name Position InterPro Accession
domain Enolpyruvate transferase domain 400 - 828 IPR001986
domain Shikimate dehydrogenase, AroM-type 1274 - 1557 IPR010110
domain Shikimate dehydrogenase substrate binding, N-terminal 1283 - 1363 IPR013708
domain 3-dehydroquinate synthase AroB 19 - 384 IPR016037
active_site 3-dehydroquinate dehydratase, active site 1141 - 1169 IPR018508
conserved_site Shikimate kinase, conserved site 914 - 941 IPR023000
conserved_site 3-phosphoshikimate 1-carboxyvinyltransferase, conserved site 480 - 494 IPR023193-1
conserved_site 3-phosphoshikimate 1-carboxyvinyltransferase, conserved site 741 - 759 IPR023193-2
domain 3-dehydroquinate synthase domain 76 - 356 IPR030960

Functions

Description
EC Number 1.1.1.25 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

7 GO annotations of molecular function

Name Definition
3-dehydroquinate dehydratase activity Catalysis of the reaction: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
3-dehydroquinate synthase activity Catalysis of the reaction: 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate.
3-phosphoshikimate 1-carboxyvinyltransferase activity Catalysis of the reaction: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
shikimate 3-dehydrogenase (NADP+) activity Catalysis of the reaction: shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+.
shikimate kinase activity Catalysis of the reaction: ATP + shikimate = 3-phosphoshikimate + ADP + 2 H(+).

4 GO annotations of biological process

Name Definition
aromatic amino acid family biosynthetic process The chemical reactions and pathways resulting in the formation of aromatic amino acid family, amino acids with aromatic ring (phenylalanine, tyrosine, tryptophan).
cellular amino acid biosynthetic process The chemical reactions and pathways resulting in the formation of amino acids, organic acids containing one or more amino substituents.
chorismate biosynthetic process The chemical reactions and pathways resulting in the formation of the unsymmetrical ether derived from phosphoenolpyruvate and 5-phosphoshikimic acid formed as an intermediate in the biosynthesis of aromatic amino acids and many other compounds.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAESSSNPTR INILGKDNII IDHGIWLNFV AQDLLQNIKS STYILITDTN LYATYVPSFQ
70 80 90 100 110 120
SVFEKAAPQD VRLLTYAIPP GEYSKGRDTK AEIEDWMLSH QCTRDTVIIA LGGGVIGDMI
130 140 150 160 170 180
GYVAATFMRG VRFVQVPTTL LAMVDSSIGG KTAIDVPMGK NLIGAFWQPE RIYIDLTFLN
190 200 210 220 230 240
TLPVREFING MAEVIKTAAI WDESEFTTLE ENAKAILEAV RSKNKSADRL APIRDILKRI
250 260 270 280 290 300
VLGSARVKAE VVSSDEREGG LRNLLNFGHS IGHAYEAILT PQVLHGEAVA IGMVKEAELA
310 320 330 340 350 360
RFLGVLKPSA VARLTKCIAS YDLPTSLQDK RIVKLTAGKE CPVDVLLQKM AVDKKNEGRK
370 380 390 400 410 420
KKIVLLSAIG KTYEPKASVV EDRAIRIVLT PCIRVHAGVP KDLKVSVTPP GSKSISNRAL
430 440 450 460 470 480
TLAALGEGTT RIYNLLHSDD TQVMLNAVAQ LQGASFSWED SDVLVVKGNG GRLQATSTPL
490 500 510 520 530 540
YLGNAGTASR FLTSVVALCN PTDVNSTVLT GNARMKQRPI GALVDALRAN GVGVKYLEKE
550 560 570 580 590 600
HSLPVQVDAA GGLAGGVMEL AATISSQYVS SLLMAAPYAR EPVTLRLVGG KPISQPYIDM
610 620 630 640 650 660
TIAMMASFGV QVQRSAEDPN TYHIPQGTYK NPETYIVESD ASSATYPLAV AAITGTTCTV
670 680 690 700 710 720
PNIGSKSLQG DARFAIEVLR PMGCTVEQTD ASTTVTGPPV GTLKAIPHVD MEPMTDAFLT
730 740 750 760 770 780
ASVLAAVASG TTQITGIANQ RVKECNRIKA MKDELAKFGV TCNELEDGIE VTGIPYTELK
790 800 810 820 830 840
NPTEGIYCYD DHRVAMSFGV LSTISPHPVL ILERECTGKT WPGWWDTMSN YFKSHLEGEE
850 860 870 880 890 900
EPHSSHVSHE KPRKGNPKSI FIIGMRGAGK STAGKWMSEV LNRPLIDLDH ELERREGQTI
910 920 930 940 950 960
PEIIRSERGW EGFRKAELDL LEDVIKNNPT GHIFSCGGGI VESEAARKLL ISYSQNGGIV
970 980 990 1000 1010 1020
LLVHRDTDQV VEYLMRDKTR PAYSENIREV YYRRKPWFEE CSNFRYYSPH PDGSKALTEP
1030 1040 1050 1060 1070 1080
PFDFSQFLSV ICGHSNHLEE AKKKPQSSFV SLTVPNVSKA LDIIPKVVVG SDAVELRVDL
1090 1100 1110 1120 1130 1140
LEDYDPEFVA KQVALLRSAA RIPIVYTVRT VSQGGKFPDD DYALALKLYR TGLQAGVEYL
1150 1160 1170 1180 1190 1200
DLEMTMPDEV IEAVTNEKGY THIIASHHDP KATLSWKNGG WIQYYNKALQ HGDVVKLVGV
1210 1220 1230 1240 1250 1260
ARELSDNFAL ARFKASLAAA HDKPFIGLNM GTAGKLSRVL NGFLTPVSHP ALPSKAAPGQ
1270 1280 1290 1300 1310 1320
LSAAEIRQAL ALIGELEPRS FYLFGKPISA SRSPALHNAL FRDNGLPHQY SLFETDNAAD
1330 1340 1350 1360 1370 1380
VKELIRATDF GGASVTIPLK LDIMPLLDEV SDAAKVIGAV NTIIPVGSGD KVTLRGDNTD
1390 1400 1410 1420 1430 1440
WMGMVYALRN AGVVKVSKES PAAGMVVGSG GTTRAAVYAL HDLGFAPIYV VARNADRIKA
1450 1460 1470 1480 1490 1500
LAESFPADYD IRSLSTPEEV AAESTAQPSV VISTIPADKP IEQSMREVLV ASLRHPSVTN
1510 1520 1530 1540 1550 1560
GKHVLLEMAY TPRHTPLMQL AEDAHWQTIP GLEVLAAQGW YQFQLWTGIT PIYTDAQAAV
MGN