ID B1Y4F8_LEPCP Unreviewed; 549 AA.
AC B1Y4F8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ACB35859.1};
DE Flags: Precursor;
GN OrderedLocusNames=Lcho_3605 {ECO:0000313|EMBL:ACB35859.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB35859.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB35859.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP001013; ACB35859.1; -; Genomic_DNA.
DR RefSeq; WP_012348606.1; NC_010524.1.
DR AlphaFoldDB; B1Y4F8; -.
DR STRING; 395495.Lcho_3605; -.
DR KEGG; lch:Lcho_3605; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_491502_0_0_4; -.
DR OrthoDB; 5476440at2; -.
DR Proteomes; UP000001693; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ACB35859.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001693};
KW Transferase {ECO:0000313|EMBL:ACB35859.1}.
SQ SEQUENCE 549 AA; 61597 MW; CF8E57D4B612B2D7 CRC64;
MDNTFALTAL ALGALAWTLP KARRRLELSR AKHRSLTGHS RMAKRVAGLI PGYAYDEQRF
FNSDGASAEI AARRKAGFDR LAALYAERYP QSAALTAQAR EGIADLQFTG NYRVPFQYSP
YLREHIKSGS FLRASSGVTV EDLDGNEFLD LTGSYGVNVF GYDFYKACID EGAARVRELG
PVLGAYHPCV LDNVKRLKAI SGLDEVSFHM SGTEAVMQAV RLARYHTRRS HLVRFCGAYH
GWWEDVQPGP GNPLPPRETY TLQDLDPRAL TVLRKRRDIA CVLINPLQAL HPNAGAPGDS
SLVDSSRRAA FDRAAYTAWL KQLREVCTER GIVLIFDEVF VGFRLAPGGA QEYFGVRADM
VTYGKTLGGG LPVGVVCGRS QWMKRFREDR PADICFARGT FNAHPYVMGA MNAFLERIEM
PDVRALYDGL DERWNARAAR FNAVLAEACL PVQVVNLSSI WTVLYTQPSR YNWMLQFYLR
AHGLALSWVG SGRLIFSLNY SDADFEAVLQ RFVAAAQAMQ ADGWWWRDAT QTNQSIRRGI
LREMLKQRF
//
