Q8RI52

PR
Gene name
ispH
Protein name
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
Names
HMBPP reductase
Species
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355)
KEGG Pathway
fnu:FN1781
EC number
1.17.7.4: With an iron-sulfur protein as acceptor
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

422-491 (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 Q8RI52

Entry ID Method Resolution Chain Position Source
AF-Q8RI52-F1 Predicted AlphaFoldDB

No variants for Q8RI52

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8RI52

No associated diseases with Q8RI52

10 regional properties for Q8RI52

Type Name Position InterPro Accession
domain S1 domain 475 - 545 IPR003029-1
domain S1 domain 559 - 632 IPR003029-2
domain S1 domain 647 - 716 IPR003029-3
domain S1 domain 730 - 802 IPR003029-4
domain RNA-binding domain, S1 307 - 373 IPR022967-1
domain RNA-binding domain, S1 389 - 460 IPR022967-2
domain RNA-binding domain, S1 475 - 545 IPR022967-3
domain RNA-binding domain, S1 560 - 632 IPR022967-4
domain RNA-binding domain, S1 647 - 716 IPR022967-5
domain RNA-binding domain, S1 731 - 802 IPR022967-6

Functions

Description
EC Number 1.17.7.4 With an iron-sulfur protein as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

4 GO annotations of molecular function

Name Definition
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity Catalysis of the reaction: (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+ = isopentenyl diphosphate + NAD(P)+ + H2O. Note that (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate is an alternative name for 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
metal ion binding Binding to a metal ion.
nucleic acid binding Binding to a nucleic acid.

3 GO annotations of biological process

Name Definition
dimethylallyl diphosphate biosynthetic process The chemical reactions and pathways resulting in the formation of dimethylallyl diphosphate.
isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway The chemical reactions and pathways resulting in the formation of isopentenyl diphosphate by the mevalonate-independent pathway. Isopentenyl diphosphate (IPP) is the fundamental unit in isoprenoid biosynthesis and is biosynthesized from pyruvate and glyceraldehyde 3-phosphate via intermediates, including 1-deoxy-D-xylulose 5-phosphate.
terpenoid biosynthetic process The chemical reactions and pathways resulting in the formation of terpenoids, any member of a class of compounds characterized by an isoprenoid chemical structure.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEIIRAKHMG FCFGVLEAIN VCNSLVEEKG RKYILGMLVH NKQVVEDMER KGFKLVTEDE
70 80 90 100 110 120
LLNDMDELKE DDIVVIRAHG TSKSVHEKLK ERKVKVFDAT CIFVNKIRQE IEIANENGYS
130 140 150 160 170 180
ILFMGDKNHP EVKGVISFAD DIQIFESFEE AKKLKIDLDK TYLLSTQTTL NKKKFEEIKK
190 200 210 220 230 240
YFKENYKNVV IFDKICGATA VRQKAVEDLA VKVEVMIIVG DTKSSNTKKL YEISKKLNDN
250 260 270 280 290 300
SYLVENEEQL DLSIFRGKEV VGITAGASTP EETIMNIEKK VRGIYKMSNV NENQNEFSLM
310 320 330 340 350 360
LEEFLPNQEK RVEGVIESMD QNFSYLDVPG ERTAVRVRTD ELKDYKVGDT VEVLITGLSE
370 380 390 400 410 420
EDDDQEYITA SRRKIEVEKN WEKIEDSFKN KTILDAKVTK KIKGGYLVEA FLYPGFLPNS
430 440 450 460 470 480
LSEISDSEEK VNGKKIQVIV KDIKMDPKDK KNRKITYSVK DIRLAEQEKE FAGLAVGQIV
490 500 510 520 530 540
DCVVTEVLDF GLAVDINTLK GFIHISEVSW KRLDKLSDNY KVGDKIKAVV VSLDEAKRNV
550 560 570 580 590 600
KLSIKKLEED PWATVANEFK VDDEIEGIVT KVLPYGAFVE IKPGVEGLVH ISDFSWTKKK
610 620 630 640 650 660
VNVADYVKER EKIKVRITDL HPEDRKLKLG IKQLVANPWE TAEKDFAIDT VIKGKVVEVK
670 680 690 700 710 720
PFGIFVEIAD GIDAFVHSSD YNWVGEEIPK FEIGNEVELK ITELDLNNKK IKGSLKALRK
730 740 750 760 770 780
SPWEHAMEEY KVGTTVEKKI KTVADFGLFI ELIKGIDGFI PTQFASKEFI KNIRDKFSEG
790 800 810 820
DVVKAQVVEV NKETQKIKLS IKKIEIEEEK REEREQIEKY STSSSEE