ID A0A1E5QCZ8_9CYAN Unreviewed; 367 AA.
AC A0A1E5QCZ8;
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=BH720_24515 {ECO:0000313|EMBL:OEJ72525.1};
OS Desertifilum tharense IPPAS B-1220.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Desertifilales; Desertifilaceae;
OC Desertifilum.
OX NCBI_TaxID=1781255 {ECO:0000313|EMBL:OEJ72525.1, ECO:0000313|Proteomes:UP000095472};
RN [1] {ECO:0000313|EMBL:OEJ72525.1, ECO:0000313|Proteomes:UP000095472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPPAS B-1220 {ECO:0000313|EMBL:OEJ72525.1,
RC ECO:0000313|Proteomes:UP000095472};
RA Sinetova M.A., Bolakhan K., Zayadan B.K., Mironov K.S., Ustinova V.,
RA Kupriyanova E.V., Sidorov R.A., Skrypnik A.N., Gogoleva N.E., Gogolev Y.V.,
RA Los D.A.;
RT "Draft genome of thermotolerant cyanobacterium Desertifilum sp. strain
RT IPPAS B-1220.";
RL Submitted (SEP-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:OEJ72525.1}.
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DR EMBL; MJGC01000122; OEJ72525.1; -; Genomic_DNA.
DR RefSeq; WP_069969864.1; NZ_MJGC01000122.1.
DR AlphaFoldDB; A0A1E5QCZ8; -.
DR STRING; 1781255.BH720_24515; -.
DR OrthoDB; 9815602at2; -.
DR Proteomes; UP000095472; 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:UP000095472};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..367
FT /note="Thiamine pyrimidine synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009184211"
FT DOMAIN 70..284
FT /note="SsuA/THI5-like"
FT /evidence="ECO:0000259|Pfam:PF09084"
SQ SEQUENCE 367 AA; 40286 MW; 67898995B925FC75 CRC64;
MAPKLYSQKF AIAIFATLAC SLMMACGSEP TTSTNVTTQS AASSTATANN PQELKTVRVS
LSWLLQGVDA PLMIAMSKGY FQEEGIEVQW ERGFGNADTI SKLGAGQYDI GFSDMYNMLE
FNDKNPNEKL VAIAVAFNKA PFSILTLKKS GIEKPEDLVG KTLGSPAGDG PRRLWPLFAK
QVGIDPDSVT WTTMDPKLRE TFLVTEEVNA ISGFSTSALP NIRKSGVKLE DVNVFYYGDY
GLDMYGNAIL IRQAFLDQNP EVAKGFVRAY LRGLKDTIEN PEAALEVVKA AGDNLIDMEA
EKLRLEIALE KLMVNAETQA NGLGSVDPKR LEETIRLTVE GFNLSRQPAL SEVFDDRFLP
PKEERSL
//
