GCH1L_STRPN
ID GCH1L_STRPN Reviewed; 265 AA.
AC Q97PK0;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
GN OrderedLocusNames=SP_1609;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC BAA-334 / TIGR4;
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of a conserved hypothetical protein from Streptococcus
RT pneumoniae TIGR4.";
RL Submitted (JUL-2011) to the PDB data bank.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC {ECO:0000305}.
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DR EMBL; AE005672; AAK75693.1; -; Genomic_DNA.
DR PIR; D95187; D95187.
DR RefSeq; WP_000881169.1; NZ_AKVY01000001.1.
DR PDB; 2FYW; X-ray; 2.40 A; A/B/C=1-265.
DR PDBsum; 2FYW; -.
DR AlphaFoldDB; Q97PK0; -.
DR SMR; Q97PK0; -.
DR STRING; 170187.SP_1609; -.
DR EnsemblBacteria; AAK75693; AAK75693; SP_1609.
DR KEGG; spn:SP_1609; -.
DR eggNOG; COG0327; Bacteria.
DR OMA; HGLFWRG; -.
DR PhylomeDB; Q97PK0; -.
DR BioCyc; SPNE170187:G1FZB-1630-MON; -.
DR EvolutionaryTrace; Q97PK0; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR002678; DUF34/NIF3.
DR InterPro; IPR036069; DUF34/NIF3_sf.
DR PANTHER; PTHR13799; PTHR13799; 1.
DR Pfam; PF01784; NIF3; 1.
DR SUPFAM; SSF102705; SSF102705; 1.
DR TIGRFAMs; TIGR00486; YbgI_SA1388; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding.
FT CHAIN 1..265
FT /note="GTP cyclohydrolase 1 type 2 homolog"
FT /id="PRO_0000147336"
FT BINDING 65
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 103
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 225
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 228
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 228
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:2FYW"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:2FYW"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:2FYW"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2FYW"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:2FYW"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:2FYW"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:2FYW"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:2FYW"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:2FYW"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:2FYW"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:2FYW"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:2FYW"
FT STRAND 132..144
FT /evidence="ECO:0007829|PDB:2FYW"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:2FYW"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2FYW"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2FYW"
FT STRAND 173..184
FT /evidence="ECO:0007829|PDB:2FYW"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2FYW"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:2FYW"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:2FYW"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:2FYW"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:2FYW"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:2FYW"
FT HELIX 230..246
FT /evidence="ECO:0007829|PDB:2FYW"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:2FYW"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:2FYW"
SQ SEQUENCE 265 AA; 29823 MW; 7FE424DD4FEE9F5C CRC64;
MLASEVIQAY EAFCPQEFSM EGDSRGLQIG TLDKGIQRVM VALDIREETV AEAIEKGVDL
IIVKHAPIFR PIKDLLASRP QNQIYIDLIK HDIAVYVSHT NIDIVENGLN DWFCQMLGIE
ETTYLQETGP ERGIGRIGNI QPQTFWELAQ QVKQVFDLDS LRMVHYQEDD LQKPISRVAI
CGGSGQSFYK DALAKGADVY ITGDIYYHTA QDMLSDGLLA LDPGHYIEVI FVEKIAALLS
QWKEDKGWSI DILPSQASTN PFHHI