ID   A0A3N4B3J5_YERPE        Unreviewed;       404 AA.
AC   A0A3N4B3J5; A0A2S9PDK9; A0A3G5L8M8; A0A5P8YHP7; Q0WDW9;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   Name=aat {ECO:0000313|EMBL:CAL21183.1};
GN   OrderedLocusNames=YPO2558 {ECO:0000313|EMBL:CAL21183.1};
GN   ORFNames=EGX46_13870 {ECO:0000313|EMBL:AYX20374.1};
OS   Yersinia pestis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632 {ECO:0000313|EMBL:CAL21183.1, ECO:0000313|Proteomes:UP000000815};
RN   [1] {ECO:0000313|EMBL:CAL21183.1, ECO:0000313|Proteomes:UP000000815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis {ECO:0000313|Proteomes:UP000000815},
RC   and CO92 {ECO:0000313|EMBL:CAL21183.1};
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Leather S., Karlyshev A.V., Moule S.,
RA   Oyston P.C.F., Quail M., Rutherford K., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2] {ECO:0000313|EMBL:CAL21183.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CO92 {ECO:0000313|EMBL:CAL21183.1};
RX   PubMed=12834539; DOI=10.1186/1471-2180-3-13;
RA   Delihas N.;
RT   "Annotation and evolutionary relationships of a small regulatory RNA gene
RT   micF and its target ompF in Yersinia species.";
RL   BMC Microbiol. 3:13-13(2003).
RN   [3] {ECO:0000313|EMBL:AYX20374.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FDAARGOS_601 {ECO:0000313|EMBL:AYX20374.1};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Jaissle J.,
RA   Tallon L.J., Sadzewicz L., Zhao X., Vavikolanu K., Mehta A.,
RA   Aluvathingal J., Nadendla S., Yan Y., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000275238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_601;
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Jaissle J.,
RA   Tallon L., Sadzewicz L., Zhao X., Vavikolanu K., Mehta A., Aluvathingal J.,
RA   Nadendla S., Yan Y., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; CP033699; AYX20374.1; -; Genomic_DNA.
DR   EMBL; AL590842; CAL21183.1; -; Genomic_DNA.
DR   PIR; AD0312; AD0312.
DR   RefSeq; WP_002210282.1; NZ_WUCM01000021.1.
DR   RefSeq; YP_002347519.1; NC_003143.1.
DR   AlphaFoldDB; A0A3N4B3J5; -.
DR   GeneID; 57976132; -.
DR   KEGG; ype:YPO2558; -.
DR   KEGG; ypj:CH55_53; -.
DR   KEGG; ypl:CH46_2557; -.
DR   KEGG; ypv:BZ15_979; -.
DR   KEGG; ypw:CH59_92; -.
DR   PATRIC; fig|214092.21.peg.2982; -.
DR   OMA; CALDLCI; -.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000275238; Chromosome.
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   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:CAL21183.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000815};
KW   Transferase {ECO:0000313|EMBL:CAL21183.1}.
FT   DOMAIN          34..393
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45541 MW;  8B0E63FBAD5C84F2 CRC64;
     MSPIEKSSKL DNVCYDIRGP VLKEAKRLEE EGNKVLKLNI GNPAPFGFDA PDEILVDVIR
     NLPTAQGYCD SKGLFSARKA IMQHYQARNI RDLTVEDIYI GNGVSELIVQ SMQALLNLGD
     EMLVPAPDYP LWTAAVSLSS GKAIHYMCDE ESGWFPDLDD IRSKITPRTR GIVIINPNNP
     TGAVYSKELL LEIVEIARQN DLIIFADEIY DKILYDDAQH HSIAALAPDL LTVTFNGLSK
     TYRVAGFRQG WMVLNGPKKH AKGYIEGLEM LASMRLCANV PMQHAIQTAL GGYQSISEFI
     QPGGRLYEQR DRAWELINQI PGVSCVKPQG ALYMFPRIDQ KRFNLKDDQK LVLDLLLQEK
     VLLVQGSAFN WPYPDHVRIV TLPRVDELEM AVRKLGRFLE TYHQ
//