ID I0I431_CALAS Unreviewed; 300 AA.
AC I0I431;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Pterin-binding domain-containing protein {ECO:0000259|PROSITE:PS50972};
GN OrderedLocusNames=CLDAP_19790 {ECO:0000313|EMBL:BAM00019.1};
OS Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS STL-6-O1).
OC Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC Caldilinea.
OX NCBI_TaxID=926550 {ECO:0000313|EMBL:BAM00019.1, ECO:0000313|Proteomes:UP000007880};
RN [1] {ECO:0000313|EMBL:BAM00019.1, ECO:0000313|Proteomes:UP000007880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC {ECO:0000313|Proteomes:UP000007880};
RA Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA Hanada S., Yamazaki S., Fujita N.;
RT "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT 102666).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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DR EMBL; AP012337; BAM00019.1; -; Genomic_DNA.
DR RefSeq; WP_014433254.1; NC_017079.1.
DR AlphaFoldDB; I0I431; -.
DR STRING; 926550.CLDAP_19790; -.
DR KEGG; cap:CLDAP_19790; -.
DR PATRIC; fig|926550.5.peg.2189; -.
DR eggNOG; COG1410; Bacteria.
DR HOGENOM; CLU_070996_0_0_0; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000007880; 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 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:UP000007880};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 20..264
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT REGION 281..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 32201 MW; 01348936E584E1E6 CRC64;
METVVSSRTK EVRIGPDLPF VIIGERINPT GRKKLAAEMA AGDFSRVISD ALAQVEAGAH
MLDVNAGIPL ADEPAILAEA IKVVQSVVDV PLAIDSSIVK ALESGLAVYQ GKALVNSVTG
EEERLEAVLP LVKKYGAAVI GISNDETGIS ENPEVRLAVA KKIIERAQDH GIPREDILID
PLVMPIGAMR YAGRQVFEIV RRCRDELKVN TCCGASNISF GLPNRGPLNA TFLAMAIGAG
LTSAITNPLE EHIRIAIKAA DVLTGNDENC MNWILSNREP RPEGEAAGSG MRRERRIRRG
//
