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Database: UniProt
Entry: A0A238WGN0_9RHOB
LinkDB: A0A238WGN0_9RHOB
Original site: A0A238WGN0_9RHOB 
ID   A0A238WGN0_9RHOB        Unreviewed;       326 AA.
AC   A0A238WGN0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171};
GN   ORFNames=SAMN06265378_104188 {ECO:0000313|EMBL:SNR45730.1};
OS   Paracoccus sediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1214787 {ECO:0000313|EMBL:SNR45730.1, ECO:0000313|Proteomes:UP000198409};
RN   [1] {ECO:0000313|Proteomes:UP000198409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26170 {ECO:0000313|Proteomes:UP000198409};
RA   Varghese N., Submissions S.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(3+) + 4 H2O + L-histidyl-[4-amino-5-hydroxymethyl-2-
CC         methylpyrimidine phosphate synthase] + N(6)-(pyridoxal phosphate)-L-
CC         lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase]
CC         = (2S)-2-amino-5-hydroxy-4-oxopentanoyl-[4-amino-5-hydroxymethyl-2-
CC         methylpyrimidine phosphate synthase] + 3-oxopropanoate + 4-amino-2-
CC         methyl-5-(phosphooxymethyl)pyrimidine + 2 Fe(2+) + 2 H(+) + L-lysyl-
CC         [4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase];
CC         Xref=Rhea:RHEA:65756, Rhea:RHEA-COMP:16892, Rhea:RHEA-COMP:16893,
CC         Rhea:RHEA-COMP:16894, Rhea:RHEA-COMP:16895, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC         ChEBI:CHEBI:29969, ChEBI:CHEBI:29979, ChEBI:CHEBI:33190,
CC         ChEBI:CHEBI:58354, ChEBI:CHEBI:143915, ChEBI:CHEBI:157692;
CC         Evidence={ECO:0000256|ARBA:ARBA00023967};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65757;
CC         Evidence={ECO:0000256|ARBA:ARBA00023967};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the NMT1/THI5 family.
CC       {ECO:0000256|ARBA:ARBA00009406}.
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DR   EMBL; FZNM01000004; SNR45730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238WGN0; -.
DR   OrthoDB; 5372616at2; -.
DR   Proteomes; UP000198409; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR027939; NMT1/THI5.
DR   InterPro; IPR015168; SsuA/THI5.
DR   PANTHER; PTHR31528; 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE PHOSPHATE SYNTHASE THI11-RELATED; 1.
DR   PANTHER; PTHR31528:SF1; 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE PHOSPHATE SYNTHASE THI11-RELATED; 1.
DR   Pfam; PF09084; NMT1; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..326
FT                   /note="Thiamine pyrimidine synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013122337"
FT   DOMAIN          32..251
FT                   /note="SsuA/THI5-like"
FT                   /evidence="ECO:0000259|Pfam:PF09084"
SQ   SEQUENCE   326 AA;  34840 MW;  B257F4F3362002D0 CRC64;
     MKALMMGAAL TLAGGAVQAQ ELTLQLKWVT QAQFAGYYVA KDKGFYEEEG LDVTILPGGP
     DIAPTQVLAG GGADVVVEWM PAALAAREKG LPLVNIAQPF KSSGMMLTCL KESGITDPAT
     DFKGKTLGVW FSGNEYPFLS WMSQLGLSTE GGPDGVTVLK QGFNVDPLLQ KQAACISTMT
     YNEYGQVLDA GIAEDDLVTF KYEDQGVATL EDGLYVLDST LQDETKVADL VKFVRASMKG
     WKYAEENPQE AAQIVLDNDE TGAQTLDHQV RMMTEIAKLT AGSDGTLDEA DYQRTVDTLM
     AGGSDPVISA APEGAFSHVV TEQAVQ
//
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