ID H5SJ96_9BACT Unreviewed; 268 AA.
AC H5SJ96;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Dihydropteroate synthase DHPS {ECO:0000313|EMBL:BAL56232.1};
GN ORFNames=HGMM_F35G12C03 {ECO:0000313|EMBL:BAL56232.1}, HGMM_F52F12C08
GN {ECO:0000313|EMBL:BAL57905.1};
OS uncultured Acetothermia bacterium.
OC Bacteria; Candidatus Bipolaricaulota; environmental samples.
OX NCBI_TaxID=236499 {ECO:0000313|EMBL:BAL56232.1};
RN [1] {ECO:0000313|EMBL:BAL56232.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAL56232.1}
RP NUCLEOTIDE SEQUENCE.
RA Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT Pathway Dominates a Subsurface Ecosystem.";
RL PLoS ONE 7:e30559-e30559(2012).
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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DR EMBL; AP011741; BAL56232.1; -; Genomic_DNA.
DR EMBL; AP011788; BAL57905.1; -; Genomic_DNA.
DR AlphaFoldDB; H5SJ96; -.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..250
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 268 AA; 29459 MW; E364EE985F88ED0A CRC64;
MILIGERING SFKDIAAAIK EKNKAPIQEW ARKQTEAGAD YLDVNLGAVS KSADDFRWLI
QTVCEAVPTP ISVDYNKLDL MKAGLEAYRE FGGGRPVIIN STTAEDSKLM PLVELAVQYN
AGLIGVVMDE RGSPQDVDRR VELGAKIFAV ASEAGLTPDR IYLDPIVMPL KFMQEQAKNV
LEAIRQFAMI SDPPPHISIG LSNICSKAKE RSLINRIFLV MAMAAGCDAA ICNVCDSELM
NAVATAELIL NKEIYSDDYL KAYRKRSL
//
