ID A0A0X8FCE3_9LACT Unreviewed; 374 AA.
AC A0A0X8FCE3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:AMB94756.1};
GN ORFNames=AWM72_08295 {ECO:0000313|EMBL:AMB94756.1};
OS Aerococcus sanguinicola.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX NCBI_TaxID=119206 {ECO:0000313|EMBL:AMB94756.1, ECO:0000313|Proteomes:UP000069912};
RN [1] {ECO:0000313|EMBL:AMB94756.1, ECO:0000313|Proteomes:UP000069912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG43001 {ECO:0000313|EMBL:AMB94756.1,
RC ECO:0000313|Proteomes:UP000069912};
RX PubMed=27103727;
RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA Christensen J.J.;
RT "Complete Genome Sequences of Aerococcus christensenii CCUG 28831T,
RT Aerococcus sanguinicola CCUG 43001T, Aerococcus urinae CCUG 36881T,
RT Aerococcus urinaeequi CCUG 28094T, Aerococcus urinaehominis CCUG 42038 BT,
RT and Aerococcus viridans CCUG 4311T.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000069912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG43001 {ECO:0000313|Proteomes:UP000069912};
RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA Christensen J.J.;
RT "Six Aerococcus type strain genome sequencing and assembly using PacBio and
RT Illumina Hiseq.";
RL Submitted (JAN-2016) 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|RuleBase:RU004075}.
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DR EMBL; CP014160; AMB94756.1; -; Genomic_DNA.
DR RefSeq; WP_067976164.1; NZ_CP014160.1.
DR AlphaFoldDB; A0A0X8FCE3; -.
DR KEGG; asan:AWM72_08295; -.
DR Proteomes; UP000069912; 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; PTHR42778; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR PANTHER; PTHR42778:SF1; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 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:AMB94756.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000069912};
KW Transferase {ECO:0000313|EMBL:AMB94756.1}.
FT DOMAIN 8..320
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 188
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 374 AA; 41231 MW; C4305CF1C4326025 CRC64;
MLNLSPGPSH VTDKVLKAFA QSKTNTDLDH DYTNYQRQVE KKVSQVLQTD APSFFMIGEA
LITLEAAIFS MVEAGDRVLV LSNGVYGAGF ADFVRFVGGR PVLFEQDWRH GIKLDELEAF
LEKDSDFQVA TFVHCETPTG ISNDIHGIGN LLHRYGILSI VDSVSGIGGE AIDFDRAQVD
VLLGGSQKCF SAPVGIGTVT LSQKALDRLD QRQSPIPSFY SNFKSYLNFD NDHFDFPYTM
SENLVYAMDA ALDQTLSHDF AAKHAKWADN TRQLFQEAGF ELYAKDHPAN TLTAVLLPEG
FSSFDVMAAV KEEGLLIANG DGPLGERILR IAHMGSNMEV EYFEAMYKAL DKAFQKVGIP
SQVSLAEAFR ASDL
//
