AAT_SACS2
ID AAT_SACS2 Reviewed; 402 AA.
AC P14909;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Aspartate aminotransferase;
DE Short=AspAT;
DE EC=2.6.1.1;
DE AltName: Full=Transaminase A;
GN Name=aspC; OrderedLocusNames=SSO0897;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-39 AND
RP 297-327.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=2513189; DOI=10.1111/j.1432-1033.1989.tb15219.x;
RA Cubellis M.V., Rozzo C., Nitti G., Arnone M.I., Marino G., Sannia G.;
RT "Cloning and sequencing of the gene coding for aspartate aminotransferase
RT from the thermoacidophilic archaebacterium Sulfolobus solfataricus.";
RL Eur. J. Biochem. 186:375-381(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP PROTEIN SEQUENCE OF 2-402, AND METHYLATION AT LYS-203 AND LYS-385.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=8026489; DOI=10.1111/j.1432-1033.1994.tb18922.x;
RA Zappacosta F., Sannia G., Savoy L.-A., Marino G., Pucci P.;
RT "Post-translational modifications in aspartate aminotransferase from
RT Sulfolobus solfataricus. Detection of N-epsilon-methyllysines by mass
RT spectrometry.";
RL Eur. J. Biochem. 222:761-767(1994).
RN [4]
RP PROTEIN SEQUENCE OF 2-23.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=3137225; DOI=10.1016/s0021-9258(18)37755-x;
RA Marino G., Nitti G., Arnone M.I., Sannia G., Gambacorta A., de Rosa M.;
RT "Purification and characterization of aspartate aminotransferase from the
RT thermoacidophilic archaebacterium Sulfolobus solfataricus.";
RL J. Biol. Chem. 263:12305-12309(1988).
RN [5]
RP PROTEIN SEQUENCE OF 240-251.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=1954227; DOI=10.1016/0167-4838(91)90002-h;
RA Birolo L., Arnone M.I., Cubellis M.V., Andreotti G., Nitti G., Marino G.,
RA Sannia G.;
RT "The active site of Sulfolobus solfataricus aspartate aminotransferase.";
RL Biochim. Biophys. Acta 1080:198-204(1991).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is above 95 degrees Celsius.;
CC -!- SUBUNIT: Homodimer.
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; X16505; CAA34514.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41178.1; -; Genomic_DNA.
DR PIR; S07088; S07088.
DR RefSeq; WP_009992318.1; NC_002754.1.
DR AlphaFoldDB; P14909; -.
DR SMR; P14909; -.
DR STRING; 273057.SSO0897; -.
DR iPTMnet; P14909; -.
DR EnsemblBacteria; AAK41178; AAK41178; SSO0897.
DR GeneID; 44129826; -.
DR KEGG; sso:SSO0897; -.
DR PATRIC; fig|273057.12.peg.899; -.
DR eggNOG; arCOG01130; Archaea.
DR HOGENOM; CLU_017584_4_3_2; -.
DR InParanoid; P14909; -.
DR OMA; SVAMTGW; -.
DR PhylomeDB; P14909; -.
DR BioCyc; MetaCyc:MON-13008; -.
DR BRENDA; 2.6.1.1; 6163.
DR Proteomes; UP000001974; 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 Aminotransferase; Cytoplasm; Direct protein sequencing; Methylation;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2513189,
FT ECO:0000269|PubMed:3137225, ECO:0000269|PubMed:8026489"
FT CHAIN 2..402
FT /note="Aspartate aminotransferase"
FT /id="PRO_0000123864"
FT BINDING 43
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 203
FT /note="N6-methyllysine; partial"
FT /evidence="ECO:0000269|PubMed:8026489"
FT MOD_RES 242
FT /note="N6-(pyridoxal phosphate)lysine"
FT MOD_RES 385
FT /note="N6-methyllysine; partial"
FT /evidence="ECO:0000269|PubMed:8026489"
SQ SEQUENCE 402 AA; 45732 MW; 99A87B354990AF0E CRC64;
MVSLLDFNGN MSQVTGETTL LYKEIARNVE KTKKIKIIDF GIGQPDLPTF KRIRDAAKEA
LDQGFTFYTS AFGIDELREK IAQYLNTRYG TDVKKEEVIV TPGAKPALFL VFILYINPSD
EVILPDPSFY SYAEVVKLLG GKPIYANLKW SREEGFSIDV DDLQSKISKR TKMIVFNNPH
NPTGTLFSPN DVKKIVDISR DNKIILLSDE IYDNFVYEGK MRSTLEDSDW RDFLIYVNGF
SKTFSMTGWR LGYIVAKREI IQKMGILAAN VYTAPTSFVQ KAAVKAFDTF DEVNQMVSLF
KKRRDVMYDE LTKVKGVEVS KPNGAFYMFP NVSKILKTSG FDVKSLAIKL IEEKGVVTIP
GEVFPLNIGK EFLRLSFAVN EEVIKEGIQK IREFAEQMMN SR
