ID D3P5P5_AZOS1 Unreviewed; 338 AA.
AC D3P5P5;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171};
GN Name=tauA {ECO:0000313|EMBL:BAI75974.1};
GN Synonyms=ssuA {ECO:0000313|EMBL:BAI75974.1};
GN OrderedLocusNames=AZL_d01480 {ECO:0000313|EMBL:BAI75974.1};
OS Azospirillum sp. (strain B510).
OG Plasmid pAB510d {ECO:0000313|EMBL:BAI75974.1,
OG ECO:0000313|Proteomes:UP000002040}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI75974.1, ECO:0000313|Proteomes:UP000002040};
RN [1] {ECO:0000313|EMBL:BAI75974.1, ECO:0000313|Proteomes:UP000002040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B510 {ECO:0000313|EMBL:BAI75974.1,
RC ECO:0000313|Proteomes:UP000002040};
RC PLASMID=pAB510d {ECO:0000313|EMBL:BAI75974.1};
RX PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA Nakayama S., Yamada M., Tabata S., Sato S.;
RT "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT sp. B510.";
RL DNA Res. 17:37-50(2010).
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; AP010950; BAI75974.1; -; Genomic_DNA.
DR RefSeq; WP_012977783.1; NC_013858.1.
DR AlphaFoldDB; D3P5P5; -.
DR KEGG; azl:AZL_d01480; -.
DR HOGENOM; CLU_028871_1_3_5; -.
DR OrthoDB; 7431968at2; -.
DR Proteomes; UP000002040; Plasmid pAB510d.
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 Plasmid {ECO:0000313|EMBL:BAI75974.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000002040};
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..338
FT /note="Thiamine pyrimidine synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003048159"
FT DOMAIN 41..259
FT /note="SsuA/THI5-like"
FT /evidence="ECO:0000259|Pfam:PF09084"
SQ SEQUENCE 338 AA; 35943 MW; D0379940E23ED319 CRC64;
MKTLASAVLL AATALTGLAG WAGPAAAADA LTLQLKWVTQ AQFAGYYVAA AKGFYKDAGL
DVTIKAGGPD INPTQVIAAG GADVIVDWMP SALASREKGV PLVNIAQIFQ KSGMMLTCRK
DANIKDPKDF KGNTLGVWFS GNEYPFLSWM SKLGYSTSGS TPDVKVLKQG FNVDPLLQKQ
AACISTMTYN EYWQLIEAGM KPAELTVFKY QDQGVATLED GLYATEKALS DPTTVEKLAK
FVKASAKGWE YAAKNQAEAV KIVLENDTTG AQTEEHQTTM MQEVAKLIEG GAKGTGYLDP
ADFDRTVGIL MSGASAPVIS KKPEGAYSHA VFDAAAKL
//
