AAPAT_CHLTE
ID AAPAT_CHLTE Reviewed; 400 AA.
AC Q8KDS8;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Aspartate/prephenate aminotransferase {ECO:0000305};
DE Short=AspAT / PAT {ECO:0000305};
DE EC=2.6.1.1 {ECO:0000269|PubMed:25070637};
DE EC=2.6.1.78 {ECO:0000269|PubMed:25070637};
GN OrderedLocusNames=CT0966 {ECO:0000312|EMBL:AAM72201.1};
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=25070637; DOI=10.1105/tpc.114.127407;
RA Dornfeld C., Weisberg A.J., Ritesh K.C., Dudareva N., Jelesko J.G.,
RA Maeda H.A.;
RT "Phylobiochemical characterization of class-Ib aspartate/prephenate
RT aminotransferases reveals evolution of the plant arogenate phenylalanine
RT pathway.";
RL Plant Cell 26:3101-3114(2014).
CC -!- FUNCTION: Catalyzes the reversible conversion of aspartate and 2-
CC oxoglutarate to glutamate and oxaloacetate (PubMed:25070637). Can also
CC transaminate prephenate in the presence of aspartate (PubMed:25070637).
CC {ECO:0000269|PubMed:25070637}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000269|PubMed:25070637};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arogenate + oxaloacetate = L-aspartate + prephenate;
CC Xref=Rhea:RHEA:20445, ChEBI:CHEBI:16452, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58180; EC=2.6.1.78;
CC Evidence={ECO:0000269|PubMed:25070637};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:25070637};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=949 uM for 2-oxoglutarate {ECO:0000269|PubMed:25070637};
CC KM=464 uM for prephenate {ECO:0000269|PubMed:25070637};
CC Note=kcat is 17.2 sec(-1) with 2-oxoglutarate as substrate. kcat is
CC 12.3 sec(-1) with prephenate as substrate.
CC {ECO:0000269|PubMed:25070637};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q56232}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AE006470; AAM72201.1; -; Genomic_DNA.
DR RefSeq; NP_661859.1; NC_002932.3.
DR RefSeq; WP_010932646.1; NC_002932.3.
DR AlphaFoldDB; Q8KDS8; -.
DR SMR; Q8KDS8; -.
DR STRING; 194439.CT0966; -.
DR EnsemblBacteria; AAM72201; AAM72201; CT0966.
DR KEGG; cte:CT0966; -.
DR PATRIC; fig|194439.7.peg.876; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_10; -.
DR OMA; SVAMTGW; -.
DR OrthoDB; 554560at2; -.
DR Proteomes; UP000001007; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033853; F:aspartate-prephenate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..400
FT /note="Aspartate/prephenate aminotransferase"
FT /id="PRO_0000448260"
FT BINDING 45
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00509"
FT BINDING 131
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 181
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 378
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT SITE 18
FT /note="Important for prephenate aminotransferase activity"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
SQ SEQUENCE 400 AA; 44007 MW; 65D5892A404237C7 CRC64;
MSVESFERFL SRRVLSMQES QTMKITGLAK KMQAEGKDVV SLSAGEPDFP TPENVCEAGI
EAIRKGFTRY TANSGIPELK KAIIRKLQRD NGLEYAEDEI IVSNGGKQAL ANTFLALCDE
GDEVIVPAPY WVSFPEMARL AEATPVIVET SIETGYKMTP EQLAAAITPK TRILVLNSPS
NPSGAVYNEA EVRALMQVIE GKEIFVLSDE MYDMICYGGV RPFSPARIPE MKPWVIVSNG
TSKSYSMTGW RIGYLAAPKW IINACDKIQS QTTSNANSIA QKAAVAALDG DQSIVEQRRA
EFEKRRDFMF RELNTISGIE CTLPEGAFYI FPSIKGLLGK TFGGKVMKDS TDVAEYLLTE
HYVATVPGDA FGAPENLRLS YAASIEELAE AVNRIRKAFS
