AAT_THEMA
ID AAT_THEMA Reviewed; 377 AA.
AC Q9X0Y2;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Aspartate aminotransferase;
DE Short=AspAT;
DE EC=2.6.1.1;
DE AltName: Full=Transaminase A;
GN Name=aspC; OrderedLocusNames=TM_1255;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP AND SUBUNIT.
RX PubMed=15103638; DOI=10.1002/prot.10646;
RA Schwarzenbacher R., Jaroszewski L., von Delft F., Abdubek P., Ambing E.,
RA Biorac T., Brinen L.S., Canaves J.M., Cambell J., Chiu H.-J., Dai X.,
RA Deacon A.M., DiDonato M., Elsliger M.-A., Eshagi S., Floyd R., Godzik A.,
RA Grittini C., Grzechnik S.K., Hampton E., Karlak C., Klock H.E., Koesema E.,
RA Kovarik J.S., Kreusch A., Kuhn P., Lesley S.A., Levin I., McMullan D.,
RA McPhillips T.M., Miller M.D., Morse A., Moy K., Ouyang J., Page R.,
RA Quijano K., Robb A., Spraggon G., Stevens R.C., van den Bedem H.,
RA Velasquez J., Vincent J., Wang X., West B., Wolf G., Xu Q., Hodgson K.O.,
RA Wooley J., Wilson I.A.;
RT "Crystal structure of an aspartate aminotransferase (TM1255) from
RT Thermotoga maritima at 1.90 A resolution.";
RL Proteins 55:759-763(2004).
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15103638}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36330.1; -; Genomic_DNA.
DR PIR; B72275; B72275.
DR RefSeq; NP_229060.1; NC_000853.1.
DR RefSeq; WP_004080007.1; NZ_CP011107.1.
DR PDB; 1O4S; X-ray; 1.90 A; A/B=1-377.
DR PDBsum; 1O4S; -.
DR AlphaFoldDB; Q9X0Y2; -.
DR SMR; Q9X0Y2; -.
DR STRING; 243274.THEMA_08060; -.
DR EnsemblBacteria; AAD36330; AAD36330; TM_1255.
DR KEGG; tma:TM1255; -.
DR eggNOG; COG0436; Bacteria.
DR InParanoid; Q9X0Y2; -.
DR OMA; IHMEVGQ; -.
DR OrthoDB; 554560at2; -.
DR EvolutionaryTrace; Q9X0Y2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 3D-structure; Aminotransferase; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..377
FT /note="Aspartate aminotransferase"
FT /id="PRO_0000123857"
FT BINDING 37
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 234
FT /note="N6-(pyridoxal phosphate)lysine"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1O4S"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:1O4S"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:1O4S"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:1O4S"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:1O4S"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 181..194
FT /evidence="ECO:0007829|PDB:1O4S"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1O4S"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:1O4S"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1O4S"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:1O4S"
FT TURN 233..237
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1O4S"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 250..263
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 269..278
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 284..303
FT /evidence="ECO:0007829|PDB:1O4S"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:1O4S"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:1O4S"
FT HELIX 360..374
FT /evidence="ECO:0007829|PDB:1O4S"
SQ SEQUENCE 377 AA; 42421 MW; 4EB507704C45E221 CRC64;
MVSRRISEIP ISKTMELDAK AKALIKKGED VINLTAGEPD FPTPEPVVEE AVRFLQKGEV
KYTDPRGIYE LREGIAKRIG ERYKKDISPD QVVVTNGAKQ ALFNAFMALL DPGDEVIVFS
PVWVSYIPQI ILAGGTVNVV ETFMSKNFQP SLEEVEGLLV GKTKAVLINS PNNPTGVVYR
REFLEGLVRL AKKRNFYIIS DEVYDSLVYT DEFTSILDVS EGFDRIVYIN GFSKSHSMTG
WRVGYLISSE KVATAVSKIQ SHTTSCINTV AQYAALKALE VDNSYMVQTF KERKNFVVER
LKKMGVKFVE PEGAFYLFFK VRGDDVKFCE RLLEEKKVAL VPGSAFLKPG FVRLSFATSI
ERLTEALDRI EDFLNSR
