ID A0A1G9D9J4_9MICO Unreviewed; 400 AA.
AC A0A1G9D9J4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=SAMN05216282_108125 {ECO:0000313|EMBL:SDK60483.1};
OS Cryobacterium psychrotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=386301 {ECO:0000313|EMBL:SDK60483.1, ECO:0000313|Proteomes:UP000198701};
RN [1] {ECO:0000313|EMBL:SDK60483.1, ECO:0000313|Proteomes:UP000198701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5382 {ECO:0000313|EMBL:SDK60483.1,
RC ECO:0000313|Proteomes:UP000198701};
RA de Groot N.N.;
RL Submitted (OCT-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|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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DR EMBL; FNFU01000008; SDK60483.1; -; Genomic_DNA.
DR STRING; 386301.SAMN05216282_108125; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000198701; 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 PRINTS; PR00753; ACCSYNTHASE.
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:SDK60483.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198701};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:SDK60483.1}.
FT DOMAIN 37..387
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 400 AA; 42694 MW; 368C733E806B6C69 CRC64;
MAHELKRIST RVGSIAESAT LKVDGKAKAL QAAGRPVISY AAGEPDFLTP EHIVEAALAA
VRDPKNYRYT PAAGLPELRE AIAAKTLRDS GLEVSPGQVV VTNGGKQAVY QAFATLLDPG
DEVLVPTPYW TTYPESIRLA GGVQVDVFAG SDQGYLVTVE QLEAARTPRT KVLLFVSPSN
PTGAVYSPEQ TRAIGEWAEE HGLWVISDEI YQNLTYDGVR AVSIVEAVPA LADRTILVNG
VAKTYAMTGW RLGWMVGPAD AIKAAANLQS HLSSNVSNIS QRAAIAALNG PQDAALAMRD
AFDRRRKIIV AELNKIPGMV TPTPQGAFYV YPDVSGLLGR TWGGVTVTTS LELADLILDQ
TEVAVVPGEA FGPSGYLRLS YALGDAPLVE GIQRLQRLFA
//
