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Database: UniProt
Entry: A0A1A5PDD8_9ACTN
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ID   A0A1A5PDD8_9ACTN        Unreviewed;       343 AA.
AC   A0A1A5PDD8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171};
GN   ORFNames=A4U61_04485 {ECO:0000313|EMBL:OBQ53450.1};
OS   Streptomyces sp. H-KF8.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1727216 {ECO:0000313|EMBL:OBQ53450.1, ECO:0000313|Proteomes:UP000093719};
RN   [1] {ECO:0000313|Proteomes:UP000093719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H-KF8 {ECO:0000313|Proteomes:UP000093719};
RA   Undabarrena A., Ugalde J.A., Seeger M., Camara B.;
RL   Submitted (APR-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBQ53450.1}.
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DR   EMBL; LWAB01000002; OBQ53450.1; -; Genomic_DNA.
DR   RefSeq; WP_065000738.1; NZ_LWAB01000002.1.
DR   AlphaFoldDB; A0A1A5PDD8; -.
DR   OrthoDB; 174578at2; -.
DR   Proteomes; UP000093719; Unassembled WGS sequence.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000093719};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..343
FT                   /note="Thiamine pyrimidine synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038947142"
FT   DOMAIN          60..268
FT                   /note="SsuA/THI5-like"
FT                   /evidence="ECO:0000259|Pfam:PF09084"
SQ   SEQUENCE   343 AA;  35193 MW;  EA0DE3EC26D992AE CRC64;
     MSRLARTVAA TALATVLTLV AGCGGSGSDT ASGADGTKAE KEKVTYLTSF GNFGRDAYAW
     VAKDKGFFEE AGFDVEIKPG QGTGGVIPAV ASGRAQFGPI DLTGGLLQMG SGRTKDFVAV
     AAIQQRTMAA IATTEGEGIT DPKDLEGKRL ADTPGSVVRS LFPTYARLAG VDASEVTWVN
     GDAQTLMGTL ASGSVDGIGQ FVVGEPTVEA VTGKKAVLLP YGDVMPDLYG NVLITSTKLA
     EEEPEMVKRF SAALLKGLEY SLAHSEEAAG ILGRNVDATN PAAAAAELDL MAAYVAPGGS
     GSTIGTLDAG RVAKSIAMLR EADALPRNVT PEQIIDFDLA PKA
//
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