ID A0A1S1MY93_9GAMM Unreviewed; 425 AA.
AC A0A1S1MY93;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
GN ORFNames=BET10_06790 {ECO:0000313|EMBL:OHU92038.1};
OS Pseudoalteromonas amylolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1859457 {ECO:0000313|EMBL:OHU92038.1, ECO:0000313|Proteomes:UP000179786};
RN [1] {ECO:0000313|EMBL:OHU92038.1, ECO:0000313|Proteomes:UP000179786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JW1 {ECO:0000313|EMBL:OHU92038.1,
RC ECO:0000313|Proteomes:UP000179786};
RA Wu Y.-H., Cheng H., Jin X.-B., Wang C.-S., Xu X.-W.;
RT "Pseudoalteromonas amylolytica sp. nov., isolated from the surface
RT seawater.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OHU92038.1}.
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DR EMBL; MKJU01000022; OHU92038.1; -; Genomic_DNA.
DR RefSeq; WP_070983840.1; NZ_MKJU01000022.1.
DR AlphaFoldDB; A0A1S1MY93; -.
DR STRING; 1859457.BET10_06790; -.
DR UniPathway; UPA00275; -.
DR Proteomes; UP000179786; Unassembled WGS sequence.
DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:InterPro.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00641; GTP_cyclohydro2; 1.
DR Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 1.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR032677; GTP_cyclohydro_II.
DR InterPro; IPR000926; RibA.
DR InterPro; IPR036144; RibA-like_sf.
DR InterPro; IPR002734; RibDG_C.
DR PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR PANTHER; PTHR21327:SF29; GTP CYCLOHYDROLASE-2; 1.
DR Pfam; PF00925; GTP_cyclohydro2; 1.
DR Pfam; PF01872; RibD_C; 1.
DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR SUPFAM; SSF142695; RibA-like; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT DOMAIN 6..166
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
FT DOMAIN 215..370
FT /note="Bacterial bifunctional deaminase-reductase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01872"
SQ SEQUENCE 425 AA; 47168 MW; 0630A3320A28B05F CRC64;
MILTASTVLP TQLGSFDVKI YRNHKGEEIT AICKGDLQGH NDLPVRMHSA CFTAEVLGSL
KCDCKQQLDF ALSYIAKHHG MVIYLPQEGR GIGLSNKIKA YALQEQGYDT IEANAMLNLP
IDARTYDDAA QIIRLHDLES VQLLTNNPLK IKQLTELGIK VTGRLPVPSD PTSHAVDYLE
TKRQQMGHML ASQNARSKTI PDPISRPFIH INFAIDGHAN TCCPNGEALS VSCNSDWQRV
HELRQKYDAI AVGANTWLND SPKLTVREEV LGREPMRQPA RIVFAGKRAA KLQNLEVDQP
NIHRATFLVG SATVRTKRGL THVNADDYLL AQPLAQLKQK KVESMLVEGG ITLIQSFVSQ
QLYDLVTIYV RTPSICKAVR LATEVLQGIC ADQIEARAFG EGILLSVVLE QSQLDARKKQ
ELAYE
//
