ID A0A5J5J9H3_9MICO Unreviewed; 376 AA.
AC A0A5J5J9H3;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE RecName: Full=4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) {ECO:0000256|HAMAP-Rule:MF_00159};
DE EC=1.17.7.3 {ECO:0000256|HAMAP-Rule:MF_00159};
DE AltName: Full=1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00159};
GN Name=ispG {ECO:0000256|HAMAP-Rule:MF_00159,
GN ECO:0000313|EMBL:KAA9111685.1};
GN Synonyms=gcpE {ECO:0000313|EMBL:KAA9111685.1};
GN ORFNames=F6B43_05665 {ECO:0000313|EMBL:KAA9111685.1};
OS Microbacterium rhizomatis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Microbacteriaceae; Microbacterium.
OX NCBI_TaxID=1631477 {ECO:0000313|EMBL:KAA9111685.1, ECO:0000313|Proteomes:UP000325827};
RN [1] {ECO:0000313|Proteomes:UP000325827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 30598 {ECO:0000313|Proteomes:UP000325827};
RA Tian Z.;
RT "Mumia zhuanghuii sp. nov. isolated from the intestinal contents of plateau
RT pika (Ochotona curzoniae) in the Qinghai-Tibet plateau of China.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate
CC (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
CC {ECO:0000256|HAMAP-Rule:MF_00159}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + oxidized
CC [flavodoxin] + H2O + 2 H(+) = 2-C-methyl-D-erythritol 2,4-cyclic
CC diphosphate + reduced [flavodoxin]; Xref=Rhea:RHEA:43604, Rhea:RHEA-
CC COMP:10622, Rhea:RHEA-COMP:10623, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:58483, ChEBI:CHEBI:128753; EC=1.17.7.3;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00159};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00159};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00159};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 5/6. {ECO:0000256|HAMAP-Rule:MF_00159}.
CC -!- SIMILARITY: Belongs to the IspG family. {ECO:0000256|HAMAP-
CC Rule:MF_00159}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA9111685.1}.
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DR EMBL; VYSA01000001; KAA9111685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5J9H3; -.
DR OrthoDB; 9803214at2; -.
DR UniPathway; UPA00056; UER00096.
DR Proteomes; UP000325827; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046429; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin); IEA:UniProtKB-UniRule.
DR GO; GO:0141197; F:4-hydroxy-3-methylbut-2-enyl-diphosphate synthase activity (flavodoxin); IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR FunFam; 3.20.20.20:FF:000001; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin); 1.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR HAMAP; MF_00159; IspG; 1.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR016425; IspG_bac.
DR InterPro; IPR004588; IspG_bac-typ.
DR InterPro; IPR058579; IspG_C.
DR InterPro; IPR058578; IspG_TIM.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR NCBIfam; TIGR00612; ispG_gcpE; 1.
DR NCBIfam; NF001540; PRK00366.1; 1.
DR PANTHER; PTHR30454; 4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR30454:SF0; 4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE (FERREDOXIN), CHLOROPLASTIC; 1.
DR Pfam; PF04551; GcpE; 1.
DR Pfam; PF26540; GcpE_C; 1.
DR PIRSF; PIRSF004640; IspG; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00159};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00159};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00159};
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW Rule:MF_00159};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00159};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00159}; Reference proteome {ECO:0000313|Proteomes:UP000325827}.
FT DOMAIN 14..254
FT /note="IspG TIM-barrel"
FT /evidence="ECO:0000259|Pfam:PF04551"
FT DOMAIN 269..355
FT /note="IspG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF26540"
FT BINDING 273
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159"
FT BINDING 276
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159"
FT BINDING 308
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159"
FT BINDING 315
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00159"
SQ SEQUENCE 376 AA; 39836 MW; 619B3EE7CEE857F6 CRC64;
MPKVAQVLAP RRKSRQIRVG KVLVGGDAPV SVQSMCTTPT TNINATLQQI AELTASGCEI
VRVAVPSQDD ADVLHIIAKK SQIPVIADIH FQPKYVFQAI DAGCAAVRVN PGNIRKFDDQ
VGAIAKAAKD AGVSLRIGVN AGSLDPRLLE KYGKATPEAL AESARWEASL FEEHDFHDFK
ISVKHNDPVI MVQAYRLLAE MGDWPLHLGV TEAGPAFQGT IKSATAFGIL LSEGIGDTIR
VSLSAPPAEE VKVGLQILQS LNLRERKLEI VSCPSCGRAQ VDVYSLADSV TEGLKDVTVP
LRVAVMGCVV NGPGEAREAD LGVASGNGKG QIFVKGQVVK TVPESEIVAT LIEEARRIAD
EMGPDAALGT AQVVTA
//
