ID   I5ASY7_EUBCE            Unreviewed;       356 AA.
AC   I5ASY7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Serine-pyruvate aminotransferase/archaeal aspartate aminotransferase {ECO:0000313|EMBL:EIM56910.1};
GN   ORFNames=EubceDRAFT1_1092 {ECO:0000313|EMBL:EIM56910.1};
OS   [Eubacterium] cellulosolvens 6.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=633697 {ECO:0000313|EMBL:EIM56910.1, ECO:0000313|Proteomes:UP000005753};
RN   [1] {ECO:0000313|EMBL:EIM56910.1, ECO:0000313|Proteomes:UP000005753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6 {ECO:0000313|EMBL:EIM56910.1,
RC   ECO:0000313|Proteomes:UP000005753};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Land M.L., Hauser L., Chang Y.-J., Anderson I.J., Johnson E.,
RA   Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EIM56910.1, ECO:0000313|Proteomes:UP000005753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6 {ECO:0000313|EMBL:EIM56910.1,
RC   ECO:0000313|Proteomes:UP000005753};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Johnson E., Mukhopadhyay B.,
RA   Anderson I., Woyke T.;
RT   "Improved High-Quality Draft sequence of Eubacterium cellulosolvens 6.";
RL   Submitted (FEB-2012) 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|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC       ECO:0000256|RuleBase:RU004075}.
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DR   EMBL; CM001487; EIM56910.1; -; Genomic_DNA.
DR   AlphaFoldDB; I5ASY7; -.
DR   STRING; 633697.EubceDRAFT1_1092; -.
DR   eggNOG; COG0075; Bacteria.
DR   HOGENOM; CLU_027686_0_1_9; -.
DR   Proteomes; UP000005753; Chromosome.
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; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR   PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:EIM56910.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000524-50}; Pyruvate {ECO:0000313|EMBL:EIM56910.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005753};
KW   Transferase {ECO:0000313|EMBL:EIM56910.1}.
FT   DOMAIN          65..322
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   BINDING         332
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT   MOD_RES         189
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ   SEQUENCE   356 AA;  39460 MW;  48C4BF6970478BCB CRC64;
     MKLMTPGPTQ VRANVLEARS RSFCNPDLDP AFYDFYKETC DLLEKALRAT DHKAFILGGE
     GILGLEAACA SLTEPGDRVL VIDNGIFGKG FADFVEIYGG EPVLFSTDPL QAVKPEELRS
     FLEKDADFKY ATMVHCDTPS GVCNDIETLS RICGEFGIMV VADSVSAMFG ERLDLGNADI
     DILCGGSQKA LSAPPGLTMI WVSTRAFAAM KNRKTPIRSF YANLLAIKDY YKNQWFPYTM
     PVSDIMGLRV ALDNFLSDPE VYDRHERVAN ATRKAVKEMG LELYLNSGMS NTVTVIKVPE
     NKSADDIIRK LRQKYGIQIA GGFDYLKGKV LRIGHMGENC RMEDVNETLE ALKNLI
//