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Database: UniProt
Entry: A0A0F7M2K3_9GAMM
LinkDB: A0A0F7M2K3_9GAMM
Original site: A0A0F7M2K3_9GAMM 
ID   A0A0F7M2K3_9GAMM        Unreviewed;       439 AA.
AC   A0A0F7M2K3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=IMCC21906_00871 {ECO:0000313|EMBL:AKH68562.1};
OS   Spongiibacter sp. IMCC21906.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; Spongiibacter.
OX   NCBI_TaxID=1620392 {ECO:0000313|EMBL:AKH68562.1, ECO:0000313|Proteomes:UP000035013};
RN   [1] {ECO:0000313|EMBL:AKH68562.1, ECO:0000313|Proteomes:UP000035013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC21906 {ECO:0000313|EMBL:AKH68562.1,
RC   ECO:0000313|Proteomes:UP000035013};
RA   Cho J.-C., Yang S.-J., Kang I.;
RT   "Complete genome sequence of IMCC21906 belonging to the
RT   Gammaproteobacteria.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP011477; AKH68562.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F7M2K3; -.
DR   STRING; 1620392.IMCC21906_00871; -.
DR   KEGG; spoi:IMCC21906_00871; -.
DR   PATRIC; fig|1620392.3.peg.926; -.
DR   Proteomes; UP000035013; Chromosome.
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; 3.40.640.10; 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   PANTHER; PTHR46383:SF2; (5-FORMYLFURAN-3-YL)METHYL PHOSPHATE TRANSAMINASE; 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:AKH68562.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035013};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:AKH68562.1}.
FT   DOMAIN          86..434
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   439 AA;  48071 MW;  AE45FF699FB4A125 CRC64;
     MPPNRQSYQI NAHHATRNCL LFVSGGFGWA SRVFELPTAV AMIATLTIAG DARVTAKFAA
     RVADIEPFRV VEVLTRAKQL ASQGRDIVHM AAGEPDFATA EPIVDAAVKA LRCGQTHYTP
     AVGIPELREA ISDYYRSDYG LDISPERIVV TPGASGALLL LSALLMAPGE GMLMADPGYP
     CNRHFLRLVE GEGQLVPVGP QDRFQLNAAL AEAAWQRNTS GVIVASPANP TGEILSRSQL
     QGLHELCQRR GGHLIVDEIY HGLSYNGAAP SILSITDDAF VINSFSKYFG MTGWRLGWIV
     APEAAVPELE KMAQNFFISP STVAQYAALA AFLPETRRIL DRRREELVQR RDFLYPALTA
     LGFDIPHKPE GAFYLYAGID KFEQSTEAFC LQLLEEHGIA ITPGIDFGKH NAQRHVRFAY
     TTSMAQLEKA VARLEALYS
//
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