ID D2TIG2_CITRI Unreviewed; 385 AA.
AC D2TIG2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Perosamine synthetase {ECO:0000313|EMBL:CBG88289.1};
GN Name=per {ECO:0000313|EMBL:CBG88289.1};
GN OrderedLocusNames=ROD_15251 {ECO:0000313|EMBL:CBG88289.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG88289.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG88289.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG88289.1,
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 -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; FN543502; CBG88289.1; -; Genomic_DNA.
DR RefSeq; WP_012905786.1; NC_013716.1.
DR AlphaFoldDB; D2TIG2; -.
DR STRING; 637910.ROD_15251; -.
DR KEGG; cro:ROD_15251; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_6_2_6; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000001889; Chromosome.
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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 191
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 385 AA; 43773 MW; C4E3E76E87E02CC1 CRC64;
MEMLPFRHRV PLLNMSLSQE EDECAANWLA KNDTKWTGKD NIQRVHQQIA QSWQTPWVAS
FMGGRAALFA IIRTLGLKPG EQILVPAFTC QCVANAISYN GVEIQFVDIE TDTYGMSAQA
LKKKLTRRTK AILIQYTFGL VCRDIDDLLS IAHQYGLWII EDCAHATGGK WRDKLLGTLG
DIAFFSSERS KIVNTLHGGW VITASPLLGE RLQAVYQQTP DADPDYIRRL LLTLRHACAG
QQKVCLPVEC DPVPQMQQAE LAGMFTAQYN WRMAEPVAEL LGLQLAKLEH ILHRRRQGAA
FWQQWAREYG FRQPVVREDA QNTWLRFPLL LTKPKAAMRG ELERLLNVET GVWFTTPIHP
QPCELPECPE GMKASKYCIN LPTWL
//
