GCH1L_ALLVD
ID GCH1L_ALLVD Reviewed; 254 AA.
AC P45371; D3RUZ0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 3.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog;
DE AltName: Full=ORF7;
GN OrderedLocusNames=Alvin_0067;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156.
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=1396692; DOI=10.1111/j.1432-1033.1992.tb17270.x;
RA Liebergesell M., Steinbuechel A.;
RT "Cloning and nucleotide sequences of genes relevant for biosynthesis of
RT poly(3-hydroxybutyric acid) in Chromatium vinosum strain D.";
RL Eur. J. Biochem. 209:135-150(1992).
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P0AFP6}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.
CC {ECO:0000305}.
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DR EMBL; CP001896; ADC61039.1; -; Genomic_DNA.
DR EMBL; L01112; AAA23326.1; -; Genomic_DNA.
DR AlphaFoldDB; P45371; -.
DR SMR; P45371; -.
DR STRING; 572477.Alvin_0067; -.
DR EnsemblBacteria; ADC61039; ADC61039; Alvin_0067.
DR KEGG; alv:Alvin_0067; -.
DR eggNOG; COG0327; Bacteria.
DR HOGENOM; CLU_037423_3_0_6; -.
DR OMA; HGLFWRG; -.
DR Proteomes; UP000001441; 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 3: Inferred from homology;
KW Metal-binding; Reference proteome.
FT CHAIN 1..254
FT /note="GTP cyclohydrolase 1 type 2 homolog"
FT /id="PRO_0000147345"
FT BINDING 68
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 69
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 106
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 222
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 226
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT BINDING 226
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFP6"
FT CONFLICT 138..156
FT /note="VGRLAQPMTPASFTEHVSQ -> AAIGSAHDACVLHGACLAS (in Ref.
FT 2; AAA23326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 27724 MW; 930D2682D8BADB9F CRC64;
MNAVMTDVRD LIRYCDDVLD AARFADYAPN GLQVEGERPL QRLVSGVTAS AALIEAAIAE
HADAILVHHG WFWKNENPCL IGIKGQRART LLSAGVSLIA YHLPLDAHPE LGNNATLGRR
LDFIDMEPTA LANGLLWVGR LAQPMTPASF TEHVSQRLAR PALRVGRETG SIERVAWCTG
GCQGYIEQAA SLGVDAFLSG ELSEQTTHQA RELGLCYLAA GHHATERYGV QALGKHLAER
FGLWHRFVEI DNPA