Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for B6JVD0

Entry ID Method Resolution Chain Position Source
AF-B6JVD0-F1 Predicted AlphaFoldDB

No variants for B6JVD0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B6JVD0

No associated diseases with B6JVD0

8 regional properties for B6JVD0

Type Name Position InterPro Accession
domain Enolpyruvate transferase domain 408 - 837 IPR001986
domain Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase 1408 - 1468 IPR006151
domain Shikimate dehydrogenase, AroM-type 1289 - 1572 IPR010110
domain Shikimate dehydrogenase substrate binding, N-terminal 1298 - 1378 IPR013708
domain 3-dehydroquinate synthase AroB 20 - 388 IPR016037
conserved_site 3-phosphoshikimate 1-carboxyvinyltransferase, conserved site 750 - 768 IPR023193
domain 3-dehydroquinate synthase domain 78 - 358 IPR030960
domain SDH, C-terminal 1546 - 1569 IPR041121

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
MSQDTDVVSV PILGKEAVFV GFNLERRVCD FLIENAKSSA YVIVTDTNIA PHYLEKYTTA
70 80 90 100 110 120
LSEAAKRHGV APRILTRVIP PGETSKCRSM KAEIEDWMLS QSCTRDTVLV AMGGGVIGDM
130 140 150 160 170 180
AGYVAATFMR GIRFIQLPTT LLAMVDSSIG GKTAIDTPNG KNLVGAFWQP LAVFADLNFL
190 200 210 220 230 240
ETLEPRQFIN GMGEVIKTAA MWNEKDFCLL EQNPTVILEA VHRPRVPGQF KFENIRNLLQ
250 260 270 280 290 300
KIILASVRTK CEVVTLDERE GGLRNLLNFG HSIGHAYEAI LFPQILHGEC VSIGMVKELE
310 320 330 340 350 360
LSRYLGILKP NAVGRVTKCL MSYTLPVSVH DAHIKKYAGY KKCPVDKLIR IMAVDKKNQG
370 380 390 400 410 420
LQKRVVILKA VGETYEKHAT VVSDEDIRVV LSHDIQVSPF DNSVSDVVVT PPGSKSISNR
430 440 450 460 470 480
ALILAAMAKG TTKLTNMLHS DDTQVMMAAL EELGAATFSW EDNGETLVVN GGGKFKTPSK
490 500 510 520 530 540
ELYLSNAGTA ARFLTTVAAL VGENEQGGEV VLTGNHRMKV RPIGPLVDAL RANGCSISYL
550 560 570 580 590 600
EREGSLPLKM IPQNGLRGGV IELAATVSSQ YVSSILMCAP YAQEPVTLKL VGGKPISQLY
610 620 630 640 650 660
VDMTIAMMKG FGVNVVKSET EAYTYHIPKA NYTSPGDYEI ESDASSATYP LAFAAITGTK
670 680 690 700 710 720
CTVPNIGSAS LQGDARFARD VLAPMGCTVE QTPTSTTVQG PPMGQLKPLE SVDMETMTDA
730 740 750 760 770 780
FLTATALAAV ACNSSGNEHI TRITGIANQR VKECNRIAAM VHELAKFGVK AGELEDGIFI
790 800 810 820 830 840
HGQSYKDLKT PEEGIYTYDD HRVAMAFSIL TLVTPKPTVI LDKACVVKTW PYWWDVLRNS
850 860 870 880 890 900
FKIKLAGVES KETVKSVKLT RSRASVILIG MRGAGKTTIG SIIAGQLNMK FLDLDQELEK
910 920 930 940 950 960
KLNTTIPDLV NTRGWDDFRQ EELQVLQEFI DTKSSDFVAA CGGGIVETPA ARELLCKYVK
970 980 990 1000 1010 1020
EGGIVLHIHR NLDQVLSYLS IDKSRPAYAD RESTKNVYLR RHQWYLDCRS HDFVSPTIES
1030 1040 1050 1060 1070 1080
GNVQSKLETS MSRFLRVVTG KSTWFEKAIQ KPHSFFLSLT FPNINDAISF LPEAIIGCDA
1090 1100 1110 1120 1130 1140
VELRADLLED PNSTTGYPSV EFVAEQFATL RAAIDLPIIF TVRSKDQGGR FPNANESEAV
1150 1160 1170 1180 1190 1200
ELMLAALRWG VDVLDLELGW STESLQAIYA RKENTKIITS WHDTAQRCSW AQPDEWLQKL
1210 1220 1230 1240 1250 1260
DMATAFGDVV KFVGIAKSMQ DNFDLEKFRK SFKGYTNKPL IAINMGTVGQ LSRVFNNVLT
1270 1280 1290 1300 1310 1320
PVTSPALPYK AAPGQLSVRQ IITALSLMGS ISPKKFYLFG TPIQHSKSPI LHKTCYDLTG
1330 1340 1350 1360 1370 1380
LPYTYDLFET ESVEGVKDVL SQPDFGGANV TIPYKLDILQ YLDELSDEAR FLGAVNTVVP
1390 1400 1410 1420 1430 1440
ISENGKRKLR GDNTDWRGIV RTFVRAGANN LNGKNALVIG AGGTSRAAIF AMHKLGAKNI
1450 1460 1470 1480 1490 1500
YLLNRTLVNA EKVKAVFPEE YNVKVIDHTK QSEISEWTKL QVAAVVSTVP ADRPLPESVS
1510 1520 1530 1540 1550 1560
KVIDALLSEI PAQKKEQYVF LDMAYKPLNT PLMSVASKHG YTCINGLEVL LQQGLASFEI
1570 1580
WTGLAVPFEH VFGLYMVLCA KEHN