ID AAT_AQUAE Reviewed; 394 AA.
AC O67781;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 01-MAY-2013, entry version 80.
DE RecName: Full=Aspartate aminotransferase;
DE Short=AspAT;
DE EC=2.6.1.1;
DE AltName: Full=Transaminase A;
GN Name=aspC; OrderedLocusNames=aq_1969;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex
RT aeolicus.";
RL Nature 392:353-358(1998).
CC -!- CATALYTIC ACTIVITY: L-aspartate + 2-oxoglutarate = oxaloacetate +
CC L-glutamate.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family.
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DR EMBL; AE000657; AAC07746.1; -; Genomic_DNA.
DR PIR; A70469; A70469.
DR RefSeq; NP_214350.1; NC_000918.1.
DR ProteinModelPortal; O67781; -.
DR SMR; O67781; 1-391.
DR STRING; 224324.aq_1969; -.
DR EnsemblBacteria; AAC07746; AAC07746; aq_1969.
DR GeneID; 1193678; -.
DR KEGG; aae:aq_1969; -.
DR PATRIC; 20960852; VBIAquAeo85532_1521.
DR eggNOG; COG0436; -.
DR HOGENOM; HOG000223062; -.
DR KO; K00812; -.
DR OMA; HTKYTPS; -.
DR ProtClustDB; CLSK2299887; -.
DR BioCyc; AAEO224324:GJBH-1411-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:EC.
DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA: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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; FALSE_NEG.
PE 3: Inferred from homology;
KW Aminotransferase; Complete proteome; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1 394 Aspartate aminotransferase.
FT /FTId=PRO_0000123833.
FT BINDING 40 40 Aspartate; via amide nitrogen (By
FT similarity).
FT BINDING 126 126 Aspartate (By similarity).
FT BINDING 176 176 Aspartate (By similarity).
FT MOD_RES 239 239 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 394 AA; 43777 MW; E570B4FD080C56E1 CRC64;
MRKGLASRVS HLKPSPTLTI TAKAKELRAK GVDVIGFGAG EPDFDTPDFI KEACIRALRE
GKTKYAPSAG IPELREAIAE KLLKENKVEY KPSEIVVSAG AKMVLFLIFM AILDEGDEVL
LPSPYWVTYP EQIRFFGGVP VEVPLKKEKG FQLSLEDVKE KVTERTKAIV INSPNNPTGA
VYEEEELKKI AEFCVERGIF IISDECYEYF VYGDAKFVSP ASFSDEVKNI TFTVNAFSKS
YSMTGWRIGY VACPEEYAKV IASLNSQSVS NVTTFAQYGA LEALKNPKSK DFVNEMRNAF
ERRRDTAVEE LSKIPGMDVV KPEGAFYIFP DFSAYAEKLG GDVKLSEFLL EKAKVAVVPG
SAFGAPGFLR LSYALSEERL VEGIRRIKKA LEEI
//
