ID R7JU54_9FIRM Unreviewed; 348 AA.
AC R7JU54;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, 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=BN630_01311 {ECO:0000313|EMBL:CDE66327.1};
OS Blautia sp. CAG:37.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1262757 {ECO:0000313|EMBL:CDE66327.1, ECO:0000313|Proteomes:UP000018204};
RN [1] {ECO:0000313|EMBL:CDE66327.1, ECO:0000313|Proteomes:UP000018204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:37 {ECO:0000313|Proteomes:UP000018204};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE66327.1}.
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DR EMBL; CBJJ010000102; CDE66327.1; -; Genomic_DNA.
DR AlphaFoldDB; R7JU54; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000018204; 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; 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.
PE 4: Predicted;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000018204}.
FT DOMAIN 17..340
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 348 AA; 39148 MW; 819C1136CEE23D5E CRC64;
MRQNPHGGDI YTKKCRVDFS VNVNPLGTPE SVKEAVRKSA ESVEQYPDAL CRDLTRALSE
KEQLPEENIL FANGAAELIF ALTQALRPKK ALIAAPGFAE YEAALSAAGC FIRMYPLQKE
KGFLLQDDFC DDLTDDLDLV FLCNPNNPTG LTIPQELLLK ILDNCRERNI YLVLDECFIE
FLPEPEKVTM QGKLDEYPNL LILRAFTKIY AMPGLRLGYL LCSDEDLLDR ISRSMQSWNV
SIPAQMAGLA ALNEDAYVKE ARELIGKERA WMKAELEKAG LTVWDSCANY LFFEGPKGLA
ARLEKGGILI RDCSNYPGLA DGYYRAAVRT HEENQILTEA VSQILQWF
//
