ID   A0A1H5MQ30_9MICO        Unreviewed;       340 AA.
AC   A0A1H5MQ30;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171};
GN   ORFNames=SAMN04488554_3545 {ECO:0000313|EMBL:SEE91323.1};
OS   Ruania alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Ruaniaceae; Ruania.
OX   NCBI_TaxID=648782 {ECO:0000313|EMBL:SEE91323.1, ECO:0000313|Proteomes:UP000199220};
RN   [1] {ECO:0000313|Proteomes:UP000199220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21368 {ECO:0000313|Proteomes:UP000199220};
RA   Varghese N., Submissions S.;
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}.
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DR   EMBL; FNTX01000002; SEE91323.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5MQ30; -.
DR   STRING; 648782.SAMN04488554_3545; -.
DR   OrthoDB; 174578at2; -.
DR   Proteomes; UP000199220; 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.
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:UP000199220};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..340
FT                   /note="Thiamine pyrimidine synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011570492"
FT   DOMAIN          56..267
FT                   /note="SsuA/THI5-like"
FT                   /evidence="ECO:0000259|Pfam:PF09084"
SQ   SEQUENCE   340 AA;  34870 MW;  A0E1BE4CD5645997 CRC64;
     MTTRHPSRRR IVAGLALSAV ASTGVLAACS DDAGTGGDAD AGVLSEASVQ LGWFPNVESA
     PIIVADENGY FADEGIDVTV EPGGPEVNSD AQIVSGNVLM GTLNSEGLAN AVIAGADLVA
     VGAIYQTSSS AIVTLADSGI EEPADLEGRR FGTSPSDDRV YPPFFELVGV GDSQIESVNI
     GADPAALVSG EVDAMSGTLA NQPIALEAQG HDVSTIRLGD YGYNRWSGVL VVRADSLEDE
     TKRATIVAML RAIAQGTADL VADPDAAAQV VVDTYGEQLG LDPDQQAASA AVWADLASGE
     AGEPVLLTDD GIASQQDFYD RVGLEVDAGT IFDTSVQEDL
//