ID   A1AML6_PELPD            Unreviewed;       381 AA.
AC   A1AML6;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   OrderedLocusNames=Ppro_0958 {ECO:0000313|EMBL:ABK98586.1};
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK98586.1, ECO:0000313|Proteomes:UP000006732};
RN   [1] {ECO:0000313|EMBL:ABK98586.1, ECO:0000313|Proteomes:UP000006732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC   {ECO:0000313|Proteomes:UP000006732};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR   EMBL; CP000482; ABK98586.1; -; Genomic_DNA.
DR   RefSeq; WP_011734893.1; NC_008609.1.
DR   AlphaFoldDB; A1AML6; -.
DR   STRING; 338966.Ppro_0958; -.
DR   KEGG; ppd:Ppro_0958; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_3_7; -.
DR   OrthoDB; 9804474at2; -.
DR   Proteomes; UP000006732; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR46383:SF2; (5-FORMYLFURAN-3-YL)METHYL PHOSPHATE TRANSAMINASE; 1.
DR   PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:ABK98586.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006732};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ABK98586.1}.
FT   DOMAIN          30..372
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   381 AA;  42541 MW;  B79D60E8AE84E485 CRC64;
     MIPERVDRMT SFIVMDVLEK AQEMERAGID VIHLEVGEPD FGVPECVSEA ISRAVRDGHT
     HYTHSLGMVE LREAICEHYG KNYGVAVHPD QVVVTSGTSP AMLSMFSTLL AKGDEVIISD
     PHYACYPNFI QFLEGKVVKV PVCEDDGFQY RPEAIRDRIT ERTRAILINS PSNPTGTVLS
     AERMWAIAQL GPYCISDEIY HGLNYHGSEH TILEFTDHAF VLNGFSKIFA MTGLRLGYLI
     APPCFIRPLQ KLQQNFFLAP NSVAQIGGIA ALKEADADVL RMRNTYDQRR RFMIQRLRDI
     GFGIPVEPTG AFYVFANAKH LSGDSYALAY DILEKARVGV TPGIDFGQGG EGYLRFTYAN
     SLENIAEGLS RLERYVAERT C
//