GenomeNet

Database: UniProt
Entry: K9XHW1_9CHRO
LinkDB: K9XHW1_9CHRO
Original site: K9XHW1_9CHRO 
ID   K9XHW1_9CHRO            Unreviewed;       348 AA.
AC   K9XHW1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=Glo7428_2751 {ECO:0000313|EMBL:AFZ31252.1};
OS   Gloeocapsa sp. PCC 7428.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Gloeocapsa.
OX   NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ31252.1, ECO:0000313|Proteomes:UP000010476};
RN   [1] {ECO:0000313|EMBL:AFZ31252.1, ECO:0000313|Proteomes:UP000010476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ31252.1,
RC   ECO:0000313|Proteomes:UP000010476};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Gloeocapsa sp. PCC 7428.";
RL   Submitted (JUN-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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003646; AFZ31252.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9XHW1; -.
DR   STRING; 1173026.Glo7428_2751; -.
DR   KEGG; glp:Glo7428_2751; -.
DR   PATRIC; fig|1173026.3.peg.2949; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_2_3; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000010476; Chromosome.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AFZ31252.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010476}.
FT   DOMAIN          22..340
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   348 AA;  38638 MW;  ECA6FC1695631069 CRC64;
     MRPIHGGNLA WAAAVAGCSP SDILDFSASI NPLGPPKSAI AAIQAHLGDL SAYPDPNYGE
     LRTALGQWHQ LPPEWILPGN GSAELLTWAG WDLAQLAKTY LYTPAFADYY RALKAFGATV
     QECPLELKIG SNVAASKCGL LLNNPHNPTG QMFLRETILP YLEQFALVVV DEAFMDFLPP
     GEEQSLIPLV QKYPNLVILR SLTKFYSLPG LRLGYAIAHP DRLQSWQQRR DPWTVNTLAA
     AAAIAAIHDS EFQQRTWAWL PPARVQLFDG LAQIPGLQPL ESTANFLLVQ CESSQILQQQ
     LLQHYKILIR DCLSFPTLGD RFFRIAVRSN EENERLLQAL FQLLAISN
//
DBGET integrated database retrieval system