ID V9G770_9BACL Unreviewed; 369 AA.
AC V9G770;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=JCM10914_1731 {ECO:0000313|EMBL:GAE05621.1};
OS Paenibacillus sp. JCM 10914.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1236974 {ECO:0000313|EMBL:GAE05621.1, ECO:0000313|Proteomes:UP000018028};
RN [1] {ECO:0000313|EMBL:GAE05621.1, ECO:0000313|Proteomes:UP000018028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10914 {ECO:0000313|EMBL:GAE05621.1,
RC ECO:0000313|Proteomes:UP000018028};
RA Ohkuma M., Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T.,
RA Hattori M.;
RT "Draft Genome Sequence of the Alkaliphilic and Xylanolytic Paenibacillus
RT sp. Strain JCM 10914, Isolated from the Gut of a Soil-Feeding Termite.";
RL Genome Announc. 2:e01144-13(2014).
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:GAE05621.1}.
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DR EMBL; BAUO01000004; GAE05621.1; -; Genomic_DNA.
DR RefSeq; WP_023959117.1; NZ_BAZR01000004.1.
DR AlphaFoldDB; V9G770; -.
DR STRING; 1236974.GCA_001315105_01691; -.
DR OrthoDB; 9813612at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000018028; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000018028}.
FT DOMAIN 32..359
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 369 AA; 40623 MW; 2DBC5A883B594192 CRC64;
MTYKDESRIE VYGHGGDIET AEATFGRRAA SFLDFSANIN PLGPPADVIT VLQESLPAVI
RYPDPGHRRF KDLLSTRIGI ARERLMAGNG AAECMALLLL GLSPKVVGVV DPCFSEYREL
SFKFGADVRS ITGHSGQDWR AGRDQVIELV QACDLLFLGQ PNNPNGVQYD LDDIRAIAEA
AERKKTWLVL DEAFIDFIPP EHRHTLLPEL HRYRQTVIIR SMTKFYAIPG LRLGYTVGHP
DVIRAMAAKQ VSWSVNGLAL LAGEACLGSG EAYERRTQEL IRTQREQLAE GLRAAGFVVA
PSEVNYLLVE VPYPWSAAAF QQELGTRGVL IRSCAMYPGL GPQHIRVAVK DAEANATLLA
VVHEVMDGV
//
