ASPAT_CORGL
ID ASPAT_CORGL Reviewed; 432 AA.
AC Q8NTR2;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Aspartate aminotransferase {ECO:0000303|PubMed:27355211};
DE Short=AspAT {ECO:0000303|PubMed:27355211};
DE EC=2.6.1.1 {ECO:0000269|PubMed:27355211};
GN OrderedLocusNames=Cgl0240 {ECO:0000312|EMBL:BAB97633.1};
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2] {ECO:0007744|PDB:3PPL}
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 7-432 IN COMPLEX WITH PYRIDOXAL
RP PHOSPHATE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of an aspartate transaminase (NCgl0237, Cgl0240) from
RT Corynebacterium glutamicum ATCC 13032 kitasato at 1.25 A resolution.";
RL Submitted (NOV-2010) to the PDB data bank.
RN [3] {ECO:0007744|PDB:5IWQ}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 7-432 IN COMPLEX WITH PYRIDOXAL
RP PHOSPHATE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND MUTAGENESIS OF
RP ARG-45; LYS-47; TYR-79; SER-109; SER-110; TYR-148; ARG-150; ASN-197;
RP ASP-226; TYR-229; SER-264; LYS-265 AND ARG-400.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=27355211; DOI=10.1371/journal.pone.0158402;
RA Son H.F., Kim K.J.;
RT "Structural insights into a novel class of aspartate aminotransferase from
RT Corynebacterium glutamicum.";
RL PLoS ONE 11:e0158402-e0158402(2016).
RN [4] {ECO:0007744|PDB:5HXX}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 7-432 IN COMPLEX WITH PYRIDOXAL
RP PHOSPHATE; 2-OXOGLUTARIC ACID AND L-GLUTAMIC ACID.
RA Son H.-F., Kim K.-J.;
RT "Structural insights into a novel class of aspartate aminotransferase from
RT Corynebacterium glutamicum.";
RL Submitted (JAN-2016) to the PDB data bank.
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:27355211};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:27355211};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27355211}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BA000036; BAB97633.1; -; Genomic_DNA.
DR RefSeq; NP_599493.1; NC_003450.3.
DR PDB; 3PPL; X-ray; 1.25 A; A/B=7-432.
DR PDB; 5HXX; X-ray; 2.00 A; A/B=7-432.
DR PDB; 5IWQ; X-ray; 2.00 A; A/B=7-432.
DR PDBsum; 3PPL; -.
DR PDBsum; 5HXX; -.
DR PDBsum; 5IWQ; -.
DR AlphaFoldDB; Q8NTR2; -.
DR SMR; Q8NTR2; -.
DR STRING; 196627.cg0294; -.
DR DNASU; 1021066; -.
DR KEGG; cgl:Cgl0240; -.
DR PATRIC; fig|196627.13.peg.245; -.
DR eggNOG; COG1167; Bacteria.
DR HOGENOM; CLU_635914_0_0_11; -.
DR OMA; AMDGVAT; -.
DR BRENDA; 2.6.1.1; 960.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR024551; AspAT_Ic.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF12897; Asp_aminotransf; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..432
FT /note="Aspartate aminotransferase"
FT /id="PRO_0000450666"
FT BINDING 45..46
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 109..111
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:27355211, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4"
FT BINDING 148..150
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 197
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:27355211, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4"
FT BINDING 229
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:27355211, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4"
FT BINDING 262..265
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:27355211, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.4"
FT MUTAGEN 45
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27355211"
FT MUTAGEN 47
FT /note="K->A: 40% decrease in activity."
FT /evidence="ECO:0000269|PubMed:27355211"
FT MUTAGEN 79
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27355211"
FT MUTAGEN 109
FT /note="S->A: 30% decrease in activity."
FT /evidence="ECO:0000269|PubMed:27355211"
FT MUTAGEN 110
FT /note="S->A: 30% decrease in activity."
FT /evidence="ECO:0000269|PubMed:27355211"
FT MUTAGEN 148
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27355211"
FT MUTAGEN 150
FT /note="R->A: 80% decrease in activity."
FT /evidence="ECO:0000269|PubMed:27355211"
FT MUTAGEN 197
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27355211"
FT MUTAGEN 226
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27355211"
FT MUTAGEN 229
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27355211"
FT MUTAGEN 264
FT /note="S->A: 30% decrease in activity."
FT /evidence="ECO:0000269|PubMed:27355211"
FT MUTAGEN 265
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27355211"
FT MUTAGEN 400
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27355211"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 17..36
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3PPL"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 110..124
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:3PPL"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:3PPL"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:3PPL"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:3PPL"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:3PPL"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:3PPL"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:3PPL"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:3PPL"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:3PPL"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:3PPL"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 280..293
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 299..309
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 312..341
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:3PPL"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:3PPL"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 367..376
FT /evidence="ECO:0007829|PDB:3PPL"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:3PPL"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:3PPL"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:3PPL"
FT HELIX 408..430
FT /evidence="ECO:0007829|PDB:3PPL"
SQ SEQUENCE 432 AA; 47296 MW; E5D1F732781444E9 CRC64;
MRRYAVMSSV SLQDFDAERI GLFHEDIKRK FDELKSKNLK LDLTRGKPSS EQLDFADELL
ALPGKGDFKA ADGTDVRNYG GLDGIVDIRQ IWADLLGVPV EQVLAGDASS LNIMFDVISW
SYIFGNNDSV QPWSKEETVK WICPVPGYDR HFSITERFGF EMISVPMNED GPDMDAVEEL
VKNPQVKGMW VVPVFSNPTG FTVTEDVAKR LSAMETAAPD FRVVWDNAYA VHTLTDEFPE
VIDIVGLGEA AGNPNRFWAF TSTSKITLAG AGVSFFLTSA ENRKWYTGHA GIRGIGPNKV
NQLAHARYFG DAEGVRAVMR KHAASLAPKF NKVLEILDSR LAEYGVAQWT VPAGGYFISL
DVVPGTASRV AELAKEAGIA LTGAGSSYPL RQDPENKNLR LAPSLPPVEE LEVAMDGVAT
CVLLAAAEHY AN
