ID A6TPS1_ALKMQ Unreviewed; 261 AA.
AC A6TPS1;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Dihydropteroate synthase, DHPS {ECO:0000313|EMBL:ABR48189.1};
GN OrderedLocusNames=Amet_2027 {ECO:0000313|EMBL:ABR48189.1};
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR48189.1, ECO:0000313|Proteomes:UP000001572};
RN [1] {ECO:0000313|Proteomes:UP000001572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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DR EMBL; CP000724; ABR48189.1; -; Genomic_DNA.
DR RefSeq; WP_012063169.1; NC_009633.1.
DR AlphaFoldDB; A6TPS1; -.
DR STRING; 293826.Amet_2027; -.
DR KEGG; amt:Amet_2027; -.
DR eggNOG; COG1410; Bacteria.
DR HOGENOM; CLU_070996_0_0_9; -.
DR OrthoDB; 9775133at2; -.
DR Proteomes; UP000001572; Chromosome.
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 NCBIfam; NF040758; CODH_ACS_meth; 1.
DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR PANTHER; PTHR45833:SF1; 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 Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000001572};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..249
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 261 AA; 28627 MW; FB996068720E9C07 CRC64;
MDKFLVIGER IHCISPAIRK ALAERDTAPI FKRAKEQIEA GADYIDVNIG PAEKDGEEIM
TWAVKAIQEE FDNVPLALDT VNRKAIEAGL KVYNKENGKA IINSADAGPR IDLFELAGQY
DAKIIGLCAK EGIPRDCEER IAYCTEMLEK AMEAGVDPDD ILFDPLFLVV KGMQEKQSDV
LEAIRQITEM GLKTTGGLSN ISNGAPKHVR PIMDAAFAAM AMQCGLSSAI INPCDKELMD
TIKTCDVVKN NILYADSYLD L
//
