ID Q8F9S7_LEPIN Unreviewed; 500 AA.
AC Q8F9S7;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:AAN47312.1};
GN Name=metC {ECO:0000313|EMBL:AAN47312.1};
GN OrderedLocusNames=LA_0113 {ECO:0000313|EMBL:AAN47312.1};
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=189518 {ECO:0000313|EMBL:AAN47312.1, ECO:0000313|Proteomes:UP000001408};
RN [1] {ECO:0000313|EMBL:AAN47312.1, ECO:0000313|Proteomes:UP000001408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601 {ECO:0000313|EMBL:AAN47312.1,
RC ECO:0000313|Proteomes:UP000001408};
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.X., Fu G., Jiang X.G., Zeng R., Miao Y.G., Xu H., Zhang Y.X.,
RA Xiong H., Lu G., Lu L.F., Jiang H.Q., Jia J., Tu Y.F., Jiang J.X., Gu W.Y.,
RA Zhang Y.Q., Cai Z., Sheng H.H., Yin H.F., Zhang Y., Zhu G.F., Wan M.,
RA Huang H.L., Qian Z., Wang S.Y., Ma W., Yao Z.J., Shen Y., Qiang B.Q.,
RA Xia Q.C., Guo X.K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.M.,
RA Shi M.H., Chen Z., Xu J.G., Zhao G.P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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DR EMBL; AE010300; AAN47312.1; -; Genomic_DNA.
DR RefSeq; NP_710294.1; NC_004342.2.
DR RefSeq; WP_000910561.1; NC_004342.2.
DR AlphaFoldDB; Q8F9S7; -.
DR STRING; 189518.LA_0113; -.
DR PaxDb; 189518-LA_0113; -.
DR EnsemblBacteria; AAN47312; AAN47312; LA_0113.
DR KEGG; lil:LA_0113; -.
DR PATRIC; fig|189518.3.peg.116; -.
DR HOGENOM; CLU_011302_2_0_12; -.
DR InParanoid; Q8F9S7; -.
DR OrthoDB; 262490at2; -.
DR Proteomes; UP000001408; Chromosome I.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42699; -; 1.
DR PANTHER; PTHR42699:SF1; CYSTATHIONINE GAMMA-SYNTHASE-RELATED; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362118};
KW Reference proteome {ECO:0000313|Proteomes:UP000001408}.
SQ SEQUENCE 500 AA; 57364 MW; 8E92BAD640249542 CRC64;
MLKEINEPHR TLCGERIPFE NIHAVSVSLP QLSDVIGYEE KRTETLSRLK SGYPRFVAHS
YIARILDYNR DTKKINTPQF IISSKKAANW IVQKFSIQNF EIIEDEGITT LVIPDLKDLE
KEILSFIQHT GCLASSRMAE DFLLKKGILQ EIFREKVEKE NPVDKILSTL SSFYGDLNPE
ILLSASGMNG VYSAFESLSL IQQKKGKTIW VRLGWLYVDN IRILEKYTES SYVIHNATDL
EELEIFLKQN SEQVAGIITE CPTNPLLLVP DYEKLKSIVD HYKIPLIVDI SVAGSAIINI
LPYVDVIVES LTKFACGNGD LMMGAVILNK NSNWFSEILP LCKEWIEKPY FRDCERLAYE
IKDYEKRVFK ISENVKKLAE FFSKQPGIRK VFWTGAIDSF QNFQKVTRLP NIHSGVLSIE
LSTSLEKFYD RLTLLKGPSF GTEFTLNMLY VYLAHYDLVI QDEGRKFLKE NGLDPNLIRI
SVGIEDPELL IEEYKKALEV
//
