ID E3D0P7_9BACT Unreviewed; 387 AA.
AC E3D0P7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Phosphoserine aminotransferase apoenzyme L-aspartate aminotransferase apoenzyme {ECO:0000313|EMBL:EFQ23868.1};
DE EC=2.6.1.1 {ECO:0000313|EMBL:EFQ23868.1};
DE EC=2.6.1.52 {ECO:0000313|EMBL:EFQ23868.1};
GN ORFNames=Apau_1449 {ECO:0000313|EMBL:EFQ23868.1};
OS Aminomonas paucivorans DSM 12260.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Aminomonas.
OX NCBI_TaxID=584708 {ECO:0000313|EMBL:EFQ23868.1, ECO:0000313|Proteomes:UP000005096};
RN [1] {ECO:0000313|EMBL:EFQ23868.1, ECO:0000313|Proteomes:UP000005096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12260 {ECO:0000313|EMBL:EFQ23868.1,
RC ECO:0000313|Proteomes:UP000005096};
RX PubMed=21304733;
RA Pitluck S., Yasawong M., Held B., Lapidus A., Nolan M., Copeland A.,
RA Lucas S., Del Rio T.G., Tice H., Cheng J.F., Chertkov O., Goodwin L.,
RA Tapia R., Han C., Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Pukall R., Spring S., Rohde M., Sikorski J., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Non-contiguous finished genome sequence of Aminomonas paucivorans type
RT strain (GLU-3).";
RL Stand. Genomic Sci. 3:285-293(2010).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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DR EMBL; CM001022; EFQ23868.1; -; Genomic_DNA.
DR RefSeq; WP_006301072.1; NZ_CM001022.1.
DR AlphaFoldDB; E3D0P7; -.
DR STRING; 584708.Apau_1449; -.
DR PaxDb; 584708-Apau_1449; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_1_1_0; -.
DR OrthoDB; 389074at2; -.
DR Proteomes; UP000005096; Chromosome.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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; 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EFQ23868.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000005096};
KW Transferase {ECO:0000313|EMBL:EFQ23868.1}.
FT DOMAIN 25..325
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 334
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 387 AA; 41647 MW; 538C64B90BFC9364 CRC64;
MQRVLLTPGP VELPDPVRLA GGNPMISHRE PAFSVLYREL LEKLARLFET SDPVLPVPGS
GTGGLDALCQ NLLEPGDEVL SVSCGAFGDR FREIAARRGV DLHVLDVPWG EAVDPASVRE
ALMARPGTKA LLLTHNETST GVVNPVEAIL AALPEPRPLV LLDGVSSVGA MSCLPQAWGV
DGLATSSQKG LMSPPGLSFL WLSSRGWEAA RSHRCPTYSL DLVLYRKDLE KNSQTPYTPP
LSLYAAVSAG LDGILREGAP VWFAARRRFA RALASGLEGL GLPLLVTREE HRSPGVTALY
FESPGVADSL RESLRSMGVE VAGGQGPLKG HLVRVAHYVD LGWPQLSLIL GSFWAACRAQ
GKLPSPKEAL ERAYETWKEE TPCGRSW
//
