GCH4_CERSK
ID GCH4_CERSK Reviewed; 359 AA.
AC B9KM22;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=GTP cyclohydrolase FolE2 {ECO:0000255|HAMAP-Rule:MF_01527};
DE EC=3.5.4.16 {ECO:0000255|HAMAP-Rule:MF_01527};
GN Name=folE2 {ECO:0000255|HAMAP-Rule:MF_01527};
GN OrderedLocusNames=RSKD131_0160;
OS Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=557760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD131 / KCTC 12085;
RX PubMed=19028901; DOI=10.1128/jb.01565-08;
RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL J. Bacteriol. 191:1118-1119(2009).
CC -!- FUNCTION: Converts GTP to 7,8-dihydroneopterin triphosphate.
CC {ECO:0000255|HAMAP-Rule:MF_01527}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate +
CC H(+); Xref=Rhea:RHEA:17473, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:37565, ChEBI:CHEBI:58462; EC=3.5.4.16;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01527};
CC -!- PATHWAY: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate
CC biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01527}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family.
CC {ECO:0000255|HAMAP-Rule:MF_01527}.
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DR EMBL; CP001150; ACM00020.1; -; Genomic_DNA.
DR RefSeq; WP_012643520.1; NC_011963.1.
DR AlphaFoldDB; B9KM22; -.
DR SMR; B9KM22; -.
DR EnsemblBacteria; ACM00020; ACM00020; RSKD131_0160.
DR GeneID; 67445641; -.
DR KEGG; rsk:RSKD131_0160; -.
DR HOGENOM; CLU_062816_0_1_5; -.
DR OMA; PCSQGMS; -.
DR UniPathway; UPA00848; UER00151.
DR Proteomes; UP000001597; Chromosome 1.
DR GO; GO:0003934; F:GTP cyclohydrolase I activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035998; P:7,8-dihydroneopterin 3'-triphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01527_B; GTP_cyclohydrol_B; 1.
DR InterPro; IPR022838; GTP_cyclohydrolase_FolE2.
DR InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR PANTHER; PTHR36445; PTHR36445; 1.
DR Pfam; PF02649; GCHY-1; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..359
FT /note="GTP cyclohydrolase FolE2"
FT /id="PRO_1000185156"
FT SITE 218
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 359 AA; 40175 MW; A32253AD8B9FFB89 CRC64;
MNILTPVAER LPSREEAEEA LAVLRRWATH TPASDVAALA PEAPALVYPE LSRSYPRAFT
VDEAYKASLP DLQNGPASLI VGAKAVIQHV GISNFRLPIR YHTRDNGDLQ LETSVTGTVS
LEAEKKGINM SRIMRSFYAH AEQAFSFEVI ERALEDYKRD LESFDARIQM RFSFPVKVPS
LRSGLTGWQY YDIALELVDR GGVRKEIMHL DFVYSSTCPC SLELSEHARR ERGQLATPHS
QRSVARISVE VRQGKCLWFE DLLDLVRSAV PTETQVMVKR EDEQAFAELN AANPIFVEDA
ARSFCQALQS DPRIGDFRVV ASHQESLHSH DAVSVLTEGP TFAAESLDPR LFSSLYHVG