MPTA_HALVD
ID MPTA_HALVD Reviewed; 308 AA.
AC D4GWJ7; A0A384KI98; L9V735;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=GTP cyclohydrolase MptA {ECO:0000255|HAMAP-Rule:MF_01527};
DE EC=3.5.4.39 {ECO:0000255|HAMAP-Rule:MF_01527};
DE AltName: Full=GTP cyclohydrolase I {ECO:0000303|PubMed:18931107, ECO:0000303|PubMed:19478918};
DE Short=GCYH-I {ECO:0000303|PubMed:18931107};
DE AltName: Full=GTP cyclohydrolase IV {ECO:0000255|HAMAP-Rule:MF_01527};
GN Name=mptA {ECO:0000255|HAMAP-Rule:MF_01527, ECO:0000312|EMBL:ADE05034.1};
GN Synonyms=folE2 {ECO:0000303|PubMed:18931107, ECO:0000303|PubMed:19478918,
GN ECO:0000312|EMBL:ADE05034.1};
GN OrderedLocusNames=HVO_2348 {ECO:0000312|EMBL:ADE05034.1};
GN ORFNames=C498_07025 {ECO:0000312|EMBL:ELY32791.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800 {ECO:0000312|EMBL:ADE05034.1};
RN [1] {ECO:0000312|EMBL:ADE05034.1, ECO:0000312|Proteomes:UP000008243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2 {ECO:0000312|Proteomes:UP000008243};
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2] {ECO:0000312|EMBL:ELY32791.1, ECO:0000312|Proteomes:UP000011532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2 {ECO:0000312|Proteomes:UP000011532};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DS2 / DS70 {ECO:0000303|PubMed:18931107};
RX PubMed=18931107; DOI=10.1128/jb.00874-08;
RA Phillips G., El Yacoubi B., Lyons B., Alvarez S., Iwata-Reuyl D.,
RA de Crecy-Lagard V.;
RT "Biosynthesis of 7-deazaguanosine-modified tRNA nucleosides: a new role for
RT GTP cyclohydrolase I.";
RL J. Bacteriol. 190:7876-7884(2008).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DS2 / DS70 {ECO:0000303|PubMed:19478918};
RX PubMed=19478918; DOI=10.1155/2009/428489;
RA El Yacoubi B., Phillips G., Blaby I.K., Haas C.E., Cruz Y., Greenberg J.,
RA de Crecy-Lagard V.;
RT "A Gateway platform for functional genomics in Haloferax volcanii: deletion
RT of three tRNA modification genes.";
RL Archaea 2:211-219(2009).
CC -!- FUNCTION: Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic
CC phosphate, the first intermediate in the biosynthesis of coenzyme
CC methanopterin (By similarity). Involved in archaeosine (G(+)) and
CC folate biosynthesis (PubMed:18931107, PubMed:19478918).
CC {ECO:0000255|HAMAP-Rule:MF_01527, ECO:0000269|PubMed:18931107,
CC ECO:0000269|PubMed:19478918}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = 7,8-dihydroneopterin 2',3'-cyclic phosphate +
CC diphosphate + formate + H(+); Xref=Rhea:RHEA:25860,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58854; EC=3.5.4.39;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01527};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01527};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01527};
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01527}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01527}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are auxotrophic for
CC thymidine (dT) and hypoxanthine (PubMed:19478918). tRNAs of the mutants
CC lack archaeosine (G(+)) (PubMed:18931107, PubMed:19478918). A slight
CC growth defect is seen in mutants grown at 45 degrees Celsius in Hv-YPC
CC (yeast-peptone-casamino acids) medium supplemented with dT
CC (PubMed:18931107). Absence of pantothenate from the growth medium of
CC the mutant cells results in a slow-growing phenotype (PubMed:19478918).
CC {ECO:0000269|PubMed:18931107, ECO:0000269|PubMed:19478918}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family.
CC {ECO:0000255|HAMAP-Rule:MF_01527}.
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DR EMBL; CP001956; ADE05034.1; -; Genomic_DNA.
DR EMBL; AOHU01000044; ELY32791.1; -; Genomic_DNA.
DR RefSeq; WP_004042238.1; NZ_AOHU01000044.1.
DR IntAct; D4GWJ7; 1.
DR STRING; 309800.C498_07025; -.
DR EnsemblBacteria; ADE05034; ADE05034; HVO_2348.
DR EnsemblBacteria; ELY32791; ELY32791; C498_07025.
DR GeneID; 8924061; -.
DR KEGG; hvo:HVO_2348; -.
DR PATRIC; fig|309800.29.peg.1357; -.
DR eggNOG; arCOG04301; Archaea.
DR HOGENOM; CLU_062816_1_0_2; -.
DR OMA; PCSQGMS; -.
DR OrthoDB; 109805at2157; -.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0003933; F:GTP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002927; P:archaeosine-tRNA biosynthetic process; IMP:UniProtKB.
DR GO; GO:0046656; P:folic acid biosynthetic process; IMP:UniProtKB.
DR HAMAP; MF_01527_A; GTP_cyclohydrol_A; 1.
DR InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA.
DR InterPro; IPR022840; GTP_cyclohydrolase_MptA.
DR PANTHER; PTHR36445; PTHR36445; 1.
DR Pfam; PF02649; GCHY-1; 1.
DR TIGRFAMs; TIGR00294; TIGR00294; 1.
PE 3: Inferred from homology;
KW Folate biosynthesis; Hydrolase; Iron; Metal-binding; Reference proteome.
FT CHAIN 1..308
FT /note="GTP cyclohydrolase MptA"
FT /id="PRO_0000454760"
FT REGION 282..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 157
FT /note="May be catalytically important"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01527"
SQ SEQUENCE 308 AA; 33516 MW; 012DA086144A1A6E CRC64;
MSHQLPDVQA SQPDVTVGLS QVGVTGVEKL VKIARDGKRP LVLMAEFEVF VDLPGGRKGI
DMSRNMQVID EVLEAAVSEP AYRVEDMCGD AAERLLAKHE YTTTAEVSMT AELVVREDTP
ASGLSTQSTA EIIASATATD EGTREEIGAE VVGMTVCPCS QGMSASRARD VLQDLAVDDD
TIEEFLDKVP QPGHSQRGHA TLTVETQGSP EVDLMDLIDI ARDSMSARIY NLAKRPDEDH
MTYHAHANAK FVEDCVRSMA ELSLEALDHL GDDAVVHMKQ SNDESIHQHN AHAEREVTLG
QLRDELDA
