GenomeNet

Database: UniProt
Entry: A0A196Q1P1_9RHOB
LinkDB: A0A196Q1P1_9RHOB
Original site: A0A196Q1P1_9RHOB 
ID   A0A196Q1P1_9RHOB        Unreviewed;       331 AA.
AC   A0A196Q1P1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171};
GN   ORFNames=A8B74_07855 {ECO:0000313|EMBL:OAN86274.1};
OS   Sulfitobacter geojensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=1342299 {ECO:0000313|EMBL:OAN86274.1, ECO:0000313|Proteomes:UP000078317};
RN   [1] {ECO:0000313|Proteomes:UP000078317}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EhN01 {ECO:0000313|Proteomes:UP000078317};
RA   Rosana A., Orata F., Boucher Y., Case R.;
RL   Submitted (MAY-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:OAN86274.1}.
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; LXYM01000044; OAN86274.1; -; Genomic_DNA.
DR   RefSeq; WP_064225001.1; NZ_LXYM01000044.1.
DR   AlphaFoldDB; A0A196Q1P1; -.
DR   STRING; 1342299.Z947_3992; -.
DR   eggNOG; COG0715; Bacteria.
DR   Proteomes; UP000078317; 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.
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:UP000078317};
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..331
FT                   /note="Thiamine pyrimidine synthase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008273717"
FT   DOMAIN          38..256
FT                   /note="SsuA/THI5-like"
FT                   /evidence="ECO:0000259|Pfam:PF09084"
SQ   SEQUENCE   331 AA;  35444 MW;  C558F9DB7093DB28 CRC64;
     MKKMMMAAAL ATGLGGAAAH ADGHANSVTL QLQWVTQAQF AGYYVALDKG FYEEEGLDVT
     VLAGGPDIAP PQVLAGGGAD AMLNWMPSAL AAREKGLPVV NIAQPFKTSG LMLTCWKDTG
     ITGPQDFKGK TIGVWFFGNE YPFLSWMSQE GISTDGGDDG VTVLKQGFNV DPLLQREADC
     ISTMTYNEYG QVLDAGVNPD ELVTFKYEEQ GVATLEDGIY VLEDNLKDPV FEDKMVRFVR
     ASMKGWKYAE ENAEEAANIV LDNDETGAQT EAAQVRMMGE IAKLTAGSNG ALVEADFQRT
     VDTLLAGGSD PVISKQPEGA WTSAITDKAL N
//
DBGET integrated database retrieval system