ID D2THV4_CITRI Unreviewed; 423 AA.
AC D2THV4;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:CBG89537.1};
GN OrderedLocusNames=ROD_27941 {ECO:0000313|EMBL:CBG89537.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG89537.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG89537.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG89537.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; FN543502; CBG89537.1; -; Genomic_DNA.
DR RefSeq; WP_012906953.1; NC_013716.1.
DR AlphaFoldDB; D2THV4; -.
DR STRING; 637910.ROD_27941; -.
DR KEGG; cro:ROD_27941; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_6; -.
DR OrthoDB; 9803354at2; -.
DR Proteomes; UP000001889; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42832:SF1; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAC; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:CBG89537.1};
KW Transferase {ECO:0000313|EMBL:CBG89537.1}.
FT DOMAIN 37..376
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 423 AA; 47082 MW; 4B43BFC073A4049E CRC64;
MADSRPERRF TRIDRLPPYV FNITAELKMA ARRRGEDIID FSMGNPDGAT PPHIVEKLCT
VAQRPDTHGY STSRGIPRLR RAISRWYQER YHVDIDPETE AIVTIGSKEG LAHLMLATLD
HGDTVLVPNP SYPIHIYGAV IAGAQVRSVP LVEGVDFFNE LERAIRESYP KPKMMILGFP
SNPTSQCVEL EFFEKVVALA KRYDVLVVHD LAYADIVYDG WKAPSIMQVP GARDVAVEFF
TLSKSYNMAG WRIGFMVGNK TLVSALARIK SYHDYGTFTP LQVAAIAALE GDQQCVRDIA
EQYKRRRDVL VKGLHEAGWM VDMPKASMYV WAKIPEQYAA MGSLEFAKKL LNEAKVCVSP
GIGFGDYGDT HVRFALIENR DRIRQAIRGI KAMFRADGLL PAAAKSASES AGQEAVAGTP
DKS
//
