ID A3VML4_9RHOB Unreviewed; 361 AA.
AC A3VML4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=GTP cyclohydrolase-2 {ECO:0000256|HAMAP-Rule:MF_00179};
DE EC=3.5.4.25 {ECO:0000256|HAMAP-Rule:MF_00179};
DE AltName: Full=GTP cyclohydrolase II {ECO:0000256|HAMAP-Rule:MF_00179};
GN Name=ribA {ECO:0000256|HAMAP-Rule:MF_00179};
GN ORFNames=RB2654_15574 {ECO:0000313|EMBL:EAQ10516.1};
OS Maritimibacter alkaliphilus HTCC2654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ10516.1, ECO:0000313|Proteomes:UP000002931};
RN [1] {ECO:0000313|EMBL:EAQ10516.1, ECO:0000313|Proteomes:UP000002931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ10516.1,
RC ECO:0000313|Proteomes:UP000002931};
RX PubMed=20729358; DOI=10.1128/JB.00873-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT genera.";
RL J. Bacteriol. 192:5552-5553(2010).
CC -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-
CC ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and
CC pyrophosphate. {ECO:0000256|ARBA:ARBA00043932, ECO:0000256|HAMAP-
CC Rule:MF_00179}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00179};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00179};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00179};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC ribitylamino)uracil from GTP: step 1/4. {ECO:0000256|ARBA:ARBA00004853,
CC ECO:0000256|HAMAP-Rule:MF_00179}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
CC {ECO:0000256|HAMAP-Rule:MF_00179}.
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:EAQ10516.1}.
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DR EMBL; AAMT01000034; EAQ10516.1; -; Genomic_DNA.
DR RefSeq; WP_008333212.1; NZ_VNHV01000002.1.
DR AlphaFoldDB; A3VML4; -.
DR STRING; 314271.RB2654_15574; -.
DR eggNOG; COG0807; Bacteria.
DR HOGENOM; CLU_020273_1_2_5; -.
DR OrthoDB; 9793111at2; -.
DR UniPathway; UPA00275; UER00400.
DR Proteomes; UP000002931; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00641; GTP_cyclohydro2; 1.
DR Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 1.
DR HAMAP; MF_00179; RibA; 1.
DR InterPro; IPR032677; GTP_cyclohydro_II.
DR InterPro; IPR000926; RibA.
DR InterPro; IPR036144; RibA-like_sf.
DR NCBIfam; TIGR00505; ribA; 1.
DR PANTHER; PTHR21327:SF18; 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 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00179};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00179};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00179};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00179}; Reference proteome {ECO:0000313|Proteomes:UP000002931};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW Rule:MF_00179}; Zinc {ECO:0000256|HAMAP-Rule:MF_00179}.
FT DOMAIN 174..337
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
FT ACT_SITE 293
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT ACT_SITE 295
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 216..220
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 237
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 259..261
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 281
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 316
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 321
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
SQ SEQUENCE 361 AA; 38433 MW; ECEABAA278136EA5 CRC64;
MTLKPTQTEL TARARADLRM GLPVVLEIGG HAGLVAAAET VDAGRLGDLR GFGPLLLAIT
PRRAATLKAR AYSDHVARVH VPRDEGVEWV LGVADPKDDL MKPMKGPLMT ERGGDEGVAR
AAIALAKSAM LLPAALVVPV DNGAEVALSH GLTRVDLTGR PDDPPVTAME EVVSACVPLE
VSEAGRLHIF RPVDGGEEHY AVEIGRPDRD HPVLARLHSA CFTGDLLGSL KCDCGPQLRA
ALAAMGENGS GVLLYLNQEG RGIGLANKMR AYSLQDQGFD TVEANHRLGF EDDERDFRIG
SEILAQMGFS AVRLMTNNPT KVAMMEANGI AVTERVPLQV GRGAHNTDYL DTKAAKSGHL
L
//
