ID A0A0Q9NBW4_9BACL Unreviewed; 368 AA.
AC A0A0Q9NBW4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=threonine-phosphate decarboxylase {ECO:0000256|ARBA:ARBA00012285};
DE EC=4.1.1.81 {ECO:0000256|ARBA:ARBA00012285};
DE AltName: Full=L-threonine-O-3-phosphate decarboxylase {ECO:0000256|ARBA:ARBA00029996};
GN ORFNames=ASL11_02900 {ECO:0000313|EMBL:KRE75788.1};
OS Paenibacillus sp. Soil750.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE75788.1, ECO:0000313|Proteomes:UP000051252};
RN [1] {ECO:0000313|EMBL:KRE75788.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE75788.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE75788.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE75788.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-
CC amino-2-propanol O-2-phosphate, the precursor for the linkage between
CC the nucleotide loop and the corrin ring in cobalamin.
CC {ECO:0000256|ARBA:ARBA00003444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + O-phospho-L-threonine = (R)-1-aminopropan-2-yl
CC phosphate + CO2; Xref=Rhea:RHEA:11492, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58563, ChEBI:CHEBI:58675; EC=4.1.1.81;
CC Evidence={ECO:0000256|ARBA:ARBA00001790};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
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:KRE75788.1}.
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DR EMBL; LMSD01000001; KRE75788.1; -; Genomic_DNA.
DR RefSeq; WP_056609424.1; NZ_LMSD01000001.1.
DR AlphaFoldDB; A0A0Q9NBW4; -.
DR STRING; 1736398.ASL11_02900; -.
DR OrthoDB; 9813612at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000051252; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0048472; F:threonine-phosphate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR005860; CobD.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01140; L_thr_O3P_dcar; 1.
DR PANTHER; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR42885:SF1; THREONINE-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 4: Predicted;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT DOMAIN 26..350
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 368 AA; 41675 MW; 627716934A9678D8 CRC64;
MLERYGHGGD LWTAEEAFNL PKEQFLDYSS NMNPLGPPEV VKEILTASWR DIVKYPDPAV
RELRRKLAQK YEIDPESILV GNGAAELIDL IIRVVKPSVT GLARPSFSEY EEAVHKTGGR
LTNISLLPEH QFELQWQDVE AALPIVDLFF LGHPNNPTGK LIPRNVLSNL LQSGRKLVLD
EAFMDFVPQE SEHSLLKLAS TNQDLIVIRS MTKFYSIPGI RLGFMVAHPD LIQQLRQQQV
QWSVNYLAQQ MGVAVLGDEA FEQSTMEWLN VEKPWLIEQL RHIGLEVVPS DVNFLLFSFP
VSSGISVKQA QKYMGRQGIL IRDASLFEGL NERYCRVAIR LREDNEGLLQ ALRRMMNDLT
RSGGTGHA
//
