ID A0A0W1A5S1_9GAMM Unreviewed; 392 AA.
AC A0A0W1A5S1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=aatA {ECO:0000313|EMBL:KTD76544.1};
GN ORFNames=Lwal_2266 {ECO:0000313|EMBL:KTD76544.1};
OS Legionella waltersii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=66969 {ECO:0000313|EMBL:KTD76544.1, ECO:0000313|Proteomes:UP000054729};
RN [1] {ECO:0000313|EMBL:KTD76544.1, ECO:0000313|Proteomes:UP000054729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51914 {ECO:0000313|EMBL:KTD76544.1,
RC ECO:0000313|Proteomes:UP000054729};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTD76544.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNZB01000051; KTD76544.1; -; Genomic_DNA.
DR RefSeq; WP_058480894.1; NZ_LT906442.1.
DR AlphaFoldDB; A0A0W1A5S1; -.
DR STRING; 66969.Lwal_2266; -.
DR PATRIC; fig|66969.6.peg.2463; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000054729; Unassembled WGS sequence.
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; 3.90.1150.10; 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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
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.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:KTD76544.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054729};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KTD76544.1}.
FT DOMAIN 33..376
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 392 AA; 42641 MW; E7C394073EF41DD5 CRC64;
MNIALAKRVQ KVKPSPTLAV AAKAAQMKAQ GLDIIGLGTG EPDFDTPQHI KLAAIAAIEA
GETKYTAVDG IPELKEAIKN KFSRDNGLDY QLNQILVSVG GKQSCYNLCQ AFLNAGDEVI
IPAPYWVSYP DMVLLADGVP VIIETTPEQR YKINAEQLEK AITPKTKMIF LNSPSNPSGV
AYTLEELKEL GKVLKNHPQV LIATDDMYEH ILWTQPFANI LNACPELYDR TIVLNGVSKA
YAMTGWRIGY AGGPAPLINA MKTIQSQSTS NPCSIAQRAA VAALNGSNDS VNEMVNAFHQ
RHDYVADRLN EIPGIEVTPA DGTFYIFPSV QSIIEQRGYA NDIEFSEKLL NEVGVALVPG
SAFGTEGCIR LSFATGIDVL KDALNRLHRF CT
//
