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AAT1_BACSU
ID   AAT1_BACSU              Reviewed;         393 AA.
AC   P53001;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Aspartate aminotransferase;
DE            Short=AspAT;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
GN   Name=aspB; OrderedLocusNames=BSU22370;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA   Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA   Serror P.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between the
RT   serA and kdg loci cloned in a yeast artificial chromosome.";
RL   Microbiology 142:2005-2016(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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:0000250}.
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; L47709; AAB38454.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14153.1; -; Genomic_DNA.
DR   PIR; C69591; C69591.
DR   RefSeq; NP_390118.1; NC_000964.3.
DR   RefSeq; WP_004398489.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P53001; -.
DR   SMR; P53001; -.
DR   IntAct; P53001; 1.
DR   MINT; P53001; -.
DR   STRING; 224308.BSU22370; -.
DR   jPOST; P53001; -.
DR   PaxDb; P53001; -.
DR   PRIDE; P53001; -.
DR   EnsemblBacteria; CAB14153; CAB14153; BSU_22370.
DR   GeneID; 939037; -.
DR   KEGG; bsu:BSU22370; -.
DR   PATRIC; fig|224308.179.peg.2441; -.
DR   eggNOG; COG0436; Bacteria.
DR   InParanoid; P53001; -.
DR   OMA; SVAMTGW; -.
DR   PhylomeDB; P53001; -.
DR   BioCyc; BSUB:BSU22370-MON; -.
DR   Proteomes; UP000001570; 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   3: Inferred from homology;
KW   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..393
FT                   /note="Aspartate aminotransferase"
FT                   /id="PRO_0000123836"
FT   BINDING         38
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         237
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   393 AA;  43088 MW;  97CDA1F389B8E13B CRC64;
     MKLAKRVSAL TPSTTLAITA KAKELKAAGH DVIGLGAGEP DFNTPQHIID AAVRSMNEGH
     TKYTPSGGLA ELKNSIAEKF KRDQNIEYKP SQIIVCTGAK HALYTLFQVI LDEEDEVIIP
     TPYWVSYPEQ VKLAGGKPVY VEGLEENHFK ISPEQLKNAI TEKTKAIVIN SPSNPTGVMY
     TEEELSALGE VCLEHDILIV SDEIYEKLTY GGKKHVSIAQ LSDRLKEQTV IINGVSKSHS
     MTGWRIGYAA GSEDIIKAMT NLASHSTSNP TSIAQYGAIA AYNGPSEPLE EMREAFEHRL
     NTIYAKLIEI PGFSCVKPEG AFYLFPNAKE AAQSCGFKDV DEFVKALLEE EKVAIVPGSG
     FGSPENVRLS YATSLDLLEE AIERIKRFVE KHS
 
 
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