ID   A0A0A2SSC1_9GAMM        Unreviewed;       499 AA.
AC   A0A0A2SSC1;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:KGP63657.1};
GN   ORFNames=EP47_03285 {ECO:0000313|EMBL:KGP63657.1};
OS   Legionella norrlandica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1498499 {ECO:0000313|EMBL:KGP63657.1, ECO:0000313|Proteomes:UP000054422};
RN   [1] {ECO:0000313|EMBL:KGP63657.1, ECO:0000313|Proteomes:UP000054422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LEGN {ECO:0000313|EMBL:KGP63657.1,
RC   ECO:0000313|Proteomes:UP000054422};
RA   Rizzardi K., Winiecka-Krusnell J., Ramliden M., Alm E., Andersson S.,
RA   Byfors S.;
RL   Submitted (MAY-2014) 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 DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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:KGP63657.1}.
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DR   EMBL; JNCF01000012; KGP63657.1; -; Genomic_DNA.
DR   RefSeq; WP_035888247.1; NZ_JNCF01000012.1.
DR   AlphaFoldDB; A0A0A2SSC1; -.
DR   STRING; 1498499.EP47_03285; -.
DR   OrthoDB; 9804264at2; -.
DR   Proteomes; UP000054422; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KGP63657.1};
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:KGP63657.1}.
FT   DOMAIN          1..60
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          65..125
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   499 AA;  56213 MW;  0AF3338D549FF118 CRC64;
     MITIKELYVN KHFSLKMALG RLDATAQGVL FLVDSDERFI RTVTDGDIRR LLLKGCTLDS
     TLEQLSEHSS KSLPVSATIQ DAYHLMKEYE LDHIPVIDEN NRPVRLIHRR ELSSNILLSS
     PHIGEHEQQY VQEAFATNWV APLGPNVDSF EKEVAEYINI KSAVALSSGT AAIHLALVLL
     DVKPGDIVFA SSFTFVATVN PIVYQGATPV FIDSDLDTWN MSPVALERAL KESKANNKMP
     KAVIIVNLYG QSANYDALCK LCDEYNVPII EDAAESLGAT YNNKYSGTFG KLGIFSFNGN
     KIITTSGGGM LVSEDESLIQ RARFLSTQAR EPVPHYEHTV VGYNYRMSNV LAGIGRGQLK
     VLEKRIKARR EIFDRYKQAL NYYPFIEMMP EIKNGFSTHW LSTLVIKPIL SKIKPEEVIE
     QLKPFNIEAR RTWKPMHRQP LFAGSKYYPH DEQFSVSDYL FDHGICLPSG SNLSSRDIDR
     VIHCLSDIFK SEQNVAEVM
//