ID A0LIV0_SYNFM Unreviewed; 398 AA.
AC A0LIV0;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=L-aspartate aminotransferase {ECO:0000313|EMBL:ABK17352.1};
DE EC=2.6.1.1 {ECO:0000313|EMBL:ABK17352.1};
GN OrderedLocusNames=Sfum_1665 {ECO:0000313|EMBL:ABK17352.1};
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK17352.1, ECO:0000313|Proteomes:UP000001784};
RN [1] {ECO:0000313|EMBL:ABK17352.1, ECO:0000313|Proteomes:UP000001784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
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., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
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 -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; CP000478; ABK17352.1; -; Genomic_DNA.
DR RefSeq; WP_011698522.1; NC_008554.1.
DR AlphaFoldDB; A0LIV0; -.
DR STRING; 335543.Sfum_1665; -.
DR KEGG; sfu:Sfum_1665; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_7; -.
DR InParanoid; A0LIV0; -.
DR OrthoDB; 9804474at2; -.
DR Proteomes; UP000001784; Chromosome.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ABK17352.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW Transferase {ECO:0000313|EMBL:ABK17352.1}.
FT DOMAIN 31..390
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 398 AA; 43560 MW; 3676F4AD2ABF1063 CRC64;
MKLAERVSRI KPSATLTINS KAKALKQSGV HVVNFGVGEP DFDTPSHIQE AAVESMRNGQ
TRYTAVGGID ELKDAVCRDI ENGYGLTYKR ENVLISCGGK HALYNLFQAV LDPGDEVIIP
SPYWVSYPDM VELAGAVPVA VPCSEQNAFK LQPEQLEKAI TSRTRLFIIN SPSNPTGTHY
TASDLKGLAE VLARHPGVLI ASDDIYCRIL FGGREWTNLA MVDERMIDRC FIINGVSKTY
CMTGWRIGYL IGNEEVIRAA TKIQGQSTSN PTSISQYASL AALNGDRRLV DQMVRTFEER
SRYVLARIGE LHGVTCPTPA GAFYVFPNFS AYFGRKVGGA SIANSLDLAD YLMEKAHVAV
VPGSPFGEDR CIRISYALSM DDLKEGFDRI GTALAALQ
//
