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Database: UniProt
Entry: A0A0M0GR85_9BACI
LinkDB: A0A0M0GR85_9BACI
Original site: A0A0M0GR85_9BACI 
ID   A0A0M0GR85_9BACI        Unreviewed;       383 AA.
AC   A0A0M0GR85;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, 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   ORFNames=AF331_07520 {ECO:0000313|EMBL:KON92288.1};
OS   Rossellomorea marisflavi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=189381 {ECO:0000313|EMBL:KON92288.1, ECO:0000313|Proteomes:UP000037405};
RN   [1] {ECO:0000313|Proteomes:UP000037405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 11544 {ECO:0000313|Proteomes:UP000037405};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-14235 jcm11544.";
RL   Submitted (JUL-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|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:KON92288.1}.
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DR   EMBL; LGUE01000001; KON92288.1; -; Genomic_DNA.
DR   RefSeq; WP_053427467.1; NZ_LGUE01000001.1.
DR   AlphaFoldDB; A0A0M0GR85; -.
DR   STRING; 189381.GCA_900166615_02770; -.
DR   GeneID; 42291783; -.
DR   PATRIC; fig|189381.12.peg.1660; -.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000037405; 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:SF4; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383; 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:KON92288.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037405};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KON92288.1}.
FT   DOMAIN          29..375
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   383 AA;  42810 MW;  9712881CEE090B40 CRC64;
     MEEKMNPRVL ELQLSGIRRF FNMVAGTEGM ISLTIGQPDF PTPLHVKEAG KRAIDENFTS
     YTHNAGMLEL RKAASDFMKE KYRLDYDEDE VIITSGASQG IDVTLRSILV EGDECILPGP
     VYPGYEPIIK LSGAKPVHID TTSNGFKLDA SLLKTAITSK TKCIILPYPS NPTGVSLTAE
     ELKEIADLIR GRGIFVVADE IYSELTFDRS HRSIAEFLRD QTIVINGLSK SHSMTGWRIG
     MVMAPKAVSQ HLLKVHQYNV SCATSVSQKA ALAALTKGKD DAIPMKDAYR KRREYVYKRL
     VGMGFRNVIK PDGAFYYFVE IPERFNGDSF EFCLELVQKE KVAVVPGEAF SVMGEGYFRL
     SYACSMEELE EGLDRMENFL ASF
//
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