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Database: UniProt
Entry: A0A0P1HP89_9RHOB
LinkDB: A0A0P1HP89_9RHOB
Original site: A0A0P1HP89_9RHOB 
ID   A0A0P1HP89_9RHOB        Unreviewed;       353 AA.
AC   A0A0P1HP89;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase {ECO:0000313|EMBL:CUH88642.1};
DE            EC=2.1.1.258 {ECO:0000313|EMBL:CUH88642.1};
GN   Name=acsE {ECO:0000313|EMBL:CUH88642.1};
GN   ORFNames=PH5382_02581 {ECO:0000313|EMBL:CUH88642.1};
OS   Phaeobacter sp. CECT 5382.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Phaeobacter.
OX   NCBI_TaxID=1712645 {ECO:0000313|EMBL:CUH88642.1, ECO:0000313|Proteomes:UP000050782};
RN   [1] {ECO:0000313|EMBL:CUH88642.1, ECO:0000313|Proteomes:UP000050782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5382 {ECO:0000313|EMBL:CUH88642.1,
RC   ECO:0000313|Proteomes:UP000050782};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) 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; CYSG01000011; CUH88642.1; -; Genomic_DNA.
DR   RefSeq; WP_058334773.1; NZ_CYSG01000011.1.
DR   AlphaFoldDB; A0A0P1HP89; -.
DR   STRING; 1712645.PH5382_02581; -.
DR   OrthoDB; 9803687at2; -.
DR   Proteomes; UP000050782; Unassembled WGS sequence.
DR   GO; GO:0102036; F:methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase activity; IEA:UniProtKB-EC.
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   ECO:0000313|EMBL:CUH88642.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050782};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUH88642.1}.
FT   DOMAIN          21..274
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
FT   REGION          323..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   353 AA;  37525 MW;  6729F376098B0496 CRC64;
     MTRTVVESKT KTAVMGFDEP FCVIGERINP TGRKKLAAEL EAGDFSTVEK DAVAQVLAGA
     TVLDINAGVV YNSNPNPNET EPPLMKKIVE LVQGLVDVPL CIDSSVPGAL EAGLEVCEGR
     PLLNSVTGEE ERLEQILPLV KKYNVPVVAI SNDDTGISED PDVRFEVAKK IVQRAADFGI
     PAHDIVVDPL VMPVGAMGTA GLQVFALVRR LREELGVNTT CGASNISFGL PNRHGINNAF
     LPMAMGAGMT SAIMNPVGLP VTQKALAAKK EEVAAAGIIL PEGMDDETFV TMFGLGSMKP
     RAGKEMEAIR AANFLTNNDP HGGEWIKFNK APAKEGEEGR GRGGRSGGRR RRA
//
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