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Database: UniProt
Entry: Q72MS4_LEPIC
LinkDB: Q72MS4_LEPIC
Original site: Q72MS4_LEPIC 
ID   Q72MS4_LEPIC            Unreviewed;       402 AA.
AC   Q72MS4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Amino-sugar biosynthesis protein {ECO:0000313|EMBL:AAS71664.1};
GN   Name=wlbF {ECO:0000313|EMBL:AAS71664.1};
GN   OrderedLocusNames=LIC_13118 {ECO:0000313|EMBL:AAS71664.1};
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=267671 {ECO:0000313|EMBL:AAS71664.1, ECO:0000313|Proteomes:UP000007037};
RN   [1] {ECO:0000313|EMBL:AAS71664.1, ECO:0000313|Proteomes:UP000007037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130 {ECO:0000313|EMBL:AAS71664.1,
RC   ECO:0000313|Proteomes:UP000007037};
RX   PubMed=15028702; DOI=10.1128/JB.186.7.2164-2172.2004;
RA   Nascimento A.L., Ko A.I., Martins E.A., Monteiro-Vitorello C.B., Ho P.L.,
RA   Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F., Leite L.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H., Harakava R., Jeronimo S.M., Junqueira-De-Azevedo I.L.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G., Lemos M.V., Marino C.L., Nunes L.R.,
RA   De Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J.,
RA   Sommer P., Tsai S.M., Simpson A.J., Ferro J.A., Camargo L.E.,
RA   Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; AE016823; AAS71664.1; -; Genomic_DNA.
DR   RefSeq; WP_001281953.1; NC_005823.1.
DR   AlphaFoldDB; Q72MS4; -.
DR   GeneID; 61142990; -.
DR   KEGG; lic:LIC_13118; -.
DR   HOGENOM; CLU_033332_0_3_12; -.
DR   Proteomes; UP000007037; Chromosome I.
DR   CDD; cd00616; AHBA_syn; 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; 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        206
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         206
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   402 AA;  45326 MW;  57DCB0169AECACF8 CRC64;
     MSDMITARKT FLPFALPCIS ERAIEEVSSV LRSGWITSGP KVKEFEEEFA RYTGADYALA
     LNSATAGLHL ALEAIGMSRE DAAICPAVTF TATAEVICYF DAEPILTDVD PIFNLMTPET
     LRDTIERECI YLNGTLFHKT TGKTVRAILP VHLAGVICDM EGILEIAKEY NLYVIEDAAH
     AFPAVRNGRK IGTFGDFTVF SFYATKGITT GEGGMVTTKH SHFAERIKLM RLHGINRETY
     DRPGWYYEVV SPGFKYNMTD VAAALGIVQL SEADELWKRR ILIAENYKRE FADLPFLHLP
     LSAPNGEHSW HLFRVEVDCA SCKMDRDIFA SELKKRNIGS SLHFIPLYEH PFYSSRFRFK
     KEHFPNANAM YARSLSIPLF PGMKDEDVQD VIRAVKEIFS AL
//
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