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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//