ID J9ZC78_LEPFM Unreviewed; 391 AA.
AC J9ZC78;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Putative pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:AFS53746.1};
GN OrderedLocusNames=LFML04_1536 {ECO:0000313|EMBL:AFS53746.1};
OS Leptospirillum ferriphilum (strain ML-04).
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1048260 {ECO:0000313|EMBL:AFS53746.1, ECO:0000313|Proteomes:UP000006177};
RN [1] {ECO:0000313|EMBL:AFS53746.1, ECO:0000313|Proteomes:UP000006177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML-04 {ECO:0000313|EMBL:AFS53746.1,
RC ECO:0000313|Proteomes:UP000006177};
RX PubMed=22203551; DOI=10.1007/s12275-011-1099-9;
RA Mi S., Song J., Lin J., Che Y., Zheng H., Lin J.;
RT "Complete genome of Leptospirillum ferriphilum ML-04 provides insight into
RT its physiology and environmental adaptation.";
RL J. Microbiol. 49:890-901(2011).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP002919; AFS53746.1; -; Genomic_DNA.
DR RefSeq; WP_014961255.1; NC_018649.1.
DR AlphaFoldDB; J9ZC78; -.
DR STRING; 1048260.LFML04_1536; -.
DR KEGG; lfi:LFML04_1536; -.
DR PATRIC; fig|1048260.3.peg.1652; -.
DR HOGENOM; CLU_033332_6_0_0; -.
DR Proteomes; UP000006177; Chromosome.
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:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 391 AA; 42882 MW; 13A50C8E6BFA1587 CRC64;
MSPIPFFDLT RQYGQVGEQV KSAVLSVLST QQFILGETVS RFEKKIADFL GTAHAAGVAS
GTDALILLLK AAGLEPGDAV LVPSFTFYAS ASSVCLAGGC PVWTEVDENR YVVSPETLEN
ALLTQCVQGP DQVYRSRQGN HPVRGIVVVH LYGQMADMEK ISAWAGSRGL WVVEDACQSI
GARLHGKSAG ILSKGAAYSF FPTKNLGGGG DGGLVTTEDA QLAERIRSLR VHGSRQRYIH
EELGYNSRLD ALQAAILEAK LEFLPGWNAR RQTLAKRYTE SFSGQDVFRA PDWNDSGDSV
YHQYTIEFRR PEDRDRVKKK MAEAGVGTEI YYPVPQHRQR AFQPYFQGDM GITDRLSSSV
LSLPIFPELT DGEQDTIIRV LLDASRQGGV S
//
