ID Q2GIH6_ANAPZ Unreviewed; 363 AA.
AC Q2GIH6;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
GN Name=ribA {ECO:0000313|EMBL:ABD43880.1};
GN OrderedLocusNames=APH_1314 {ECO:0000313|EMBL:ABD43880.1};
OS Anaplasma phagocytophilum (strain HZ).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma; phagocytophilum group.
OX NCBI_TaxID=212042 {ECO:0000313|EMBL:ABD43880.1, ECO:0000313|Proteomes:UP000001943};
RN [1] {ECO:0000313|EMBL:ABD43880.1, ECO:0000313|Proteomes:UP000001943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ {ECO:0000313|EMBL:ABD43880.1,
RC ECO:0000313|Proteomes:UP000001943};
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-
CC pyrimidine + formate + 3 H(+) + 2 phosphate; Xref=Rhea:RHEA:23704,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58614; EC=3.5.4.25;
CC Evidence={ECO:0000256|ARBA:ARBA00029293};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005104}.
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DR EMBL; CP000235; ABD43880.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2GIH6; -.
DR STRING; 212042.APH_1314; -.
DR PaxDb; 212042-APH_1314; -.
DR EnsemblBacteria; ABD43880; ABD43880; APH_1314.
DR KEGG; aph:APH_1314; -.
DR PATRIC; fig|212042.8.peg.1408; -.
DR eggNOG; COG0108; Bacteria.
DR eggNOG; COG0807; Bacteria.
DR HOGENOM; CLU_020273_1_2_5; -.
DR UniPathway; UPA00275; -.
DR Proteomes; UP000001943; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00641; GTP_cyclohydro2; 1.
DR Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 1.
DR InterPro; IPR032677; GTP_cyclohydro_II.
DR InterPro; IPR000926; RibA.
DR InterPro; IPR036144; RibA-like_sf.
DR PANTHER; PTHR21327:SF46; 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR Pfam; PF00925; GTP_cyclohydro2; 1.
DR SUPFAM; SSF142695; RibA-like; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABD43880.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT DOMAIN 187..339
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
SQ SEQUENCE 363 AA; 40352 MW; EC4430DE01DB0882 CRC64;
MFGPIGNFFG LGNNLLSRAV NEIRRCAPVI LHEDDKYLLV FASELLEEPS LAVFKSFSDN
VYILLTAQRA SYVTTNDKLS RVGANTLSLA DIRTLMSGLP EETRSVPVEE SLSPLDSLAI
DLVKMAKLLP SALVIDMGFG NIEEMYDWCK CNGILHLAGK ALTDYTQEYV LQEVCRSDLY
LQDSLKSKII VYRSKIGEPE HYAIVIGEPA IENIVVRLHS SCYTGDLLGS LSCDCRSQLL
TAVKLLAEQA GGIILYISQE GRGIGLANKI RAYSLQMQNS LDTVDANRFL GFDDDERIFL
PAAMILRNLG VSSLQLLTNN PHKVQEIGKY GFDVTKTIPF HMEINEYNGN YIKTKQTRLG
HTN
//
