GenomeNet

Database: UniProt
Entry: A0A1G7TLZ3_9MICO
LinkDB: A0A1G7TLZ3_9MICO
Original site: A0A1G7TLZ3_9MICO 
ID   A0A1G7TLZ3_9MICO        Unreviewed;       389 AA.
AC   A0A1G7TLZ3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171};
GN   ORFNames=SAMN04489810_0099 {ECO:0000313|EMBL:SDG36348.1};
OS   Microbacterium pygmaeum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=370764 {ECO:0000313|EMBL:SDG36348.1, ECO:0000313|Proteomes:UP000199009};
RN   [1] {ECO:0000313|EMBL:SDG36348.1, ECO:0000313|Proteomes:UP000199009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23142 {ECO:0000313|EMBL:SDG36348.1,
RC   ECO:0000313|Proteomes:UP000199009};
RA   de Groot N.N.;
RL   Submitted (OCT-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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT629692; SDG36348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7TLZ3; -.
DR   STRING; 370764.SAMN04489810_0099; -.
DR   OrthoDB; 174578at2; -.
DR   Proteomes; UP000199009; Chromosome i.
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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 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:UP000199009};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..389
FT                   /note="Thiamine pyrimidine synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009242670"
FT   DOMAIN          56..279
FT                   /note="SsuA/THI5-like"
FT                   /evidence="ECO:0000259|Pfam:PF09084"
SQ   SEQUENCE   389 AA;  41770 MW;  ACB6661E4D2DE9FE CRC64;
     MRHRTRRLLA ITGAAAVTAL ALAACSAPAP EATTGADGDF EPITDIKLQL QWLPQAQFAG
     YYVALDQGYF EEEGFDSVEI VPSGGDIVPQ DALVAGDVDF AIAWVPKVLG TLEATGVELT
     DIAQVYQKSG TLQVSWAGDG IESVADFEGK RIGSWGFGNE WEIFAAMAAD DLDASGVSIT
     TQDFSMNALL DRDVDAAQAM TYNEWAQILE VVNPATGELY QPEDFDVISY EDTDGAMLQD
     AIWADTQRLE DPAYADAAVR FLKAVTKGWV FARDNPEEAA SITYDAAINA EAAFPVGPVH
     QQWQMNEVNK LIWAGGDFGI VDEAAWDKTV AGALSAKNQD GLELITTEPA DSAYSNTYIE
     QALAELKDEG VEVGGEYTPI DVVLTEGGQ
//
DBGET integrated database retrieval system