ID D5AV15_RHOCB Unreviewed; 320 AA.
AC D5AV15;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 Name=cobC {ECO:0000313|EMBL:ADE85797.1};
GN OrderedLocusNames=RCAP_rcc02053 {ECO:0000313|EMBL:ADE85797.1};
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=272942 {ECO:0000313|EMBL:ADE85797.1, ECO:0000313|Proteomes:UP000002361};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SB1003;
RA Strnad H., Lapidus A., Vlcek C., Ulbrich P., Paces J., Maltsev N.,
RA Kumar V., Kogan Y., Milgram A., Rebrekov D., Mazur M., Cox R., Kyrpides N.,
RA Kolar M., Sachova J., Ridl J., Ivanova N., Kapatral V., Los T., Lykidis A.,
RA Mikhailova N., Reznik G., Vasieva O., Fonstein M., Paces V., Haselkorn R.;
RT "Complete genome sequence of Rhodobacter capsulatus SB1003.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADE85797.1, ECO:0000313|Proteomes:UP000002361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003
RC {ECO:0000313|Proteomes:UP000002361};
RX PubMed=20418398; DOI=10.1128/JB.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
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}.
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DR EMBL; CP001312; ADE85797.1; -; Genomic_DNA.
DR RefSeq; WP_013067776.1; NC_014034.1.
DR AlphaFoldDB; D5AV15; -.
DR STRING; 272942.RCAP_rcc02053; -.
DR GeneID; 31490915; -.
DR KEGG; rcp:RCAP_rcc02053; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_4_5; -.
DR OrthoDB; 9799304at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002361; 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: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, ECO:0000313|EMBL:ADE85797.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002361}.
FT DOMAIN 56..304
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 320 AA; 33893 MW; CE55A758465571D6 CRC64;
MRDHGGNSDA ARAQYGGEDW IDLSTGINRQ PWPVPDLPAH VWTDLPTATA KAALLDAAAA
AFGTPAPGVA LAGAQQAIQL IPRLWAPGRA RVLGPTYNEH AAALRAAGWQ VEEVSTLGAL
AGADLAVVVN PNNPDGQRHP AAALRALSLQ VGRLVVDESF ADASPAASVT AKASRRMLVL
RSFGKFYGLA GLRLGFVFAD AATVAALSEM AGPWPVSGPA LEIGRRALLD RNWAMATALR
LGAETMRMDA LAARAGWRLV GGTALFRTYA TPDAAAAQDH LARARIWSRV FPYAADWLRL
GLPGNESEWM RLEKALTNEL
//
