ID A9BDE9_PROM4 Unreviewed; 376 AA.
AC A9BDE9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=P9211_02041 {ECO:0000313|EMBL:ABX08135.1};
OS Prochlorococcus marinus (strain MIT 9211).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=93059 {ECO:0000313|EMBL:ABX08135.1, ECO:0000313|Proteomes:UP000000788};
RN [1] {ECO:0000313|EMBL:ABX08135.1, ECO:0000313|Proteomes:UP000000788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9211 {ECO:0000313|Proteomes:UP000000788};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000878; ABX08135.1; -; Genomic_DNA.
DR RefSeq; WP_012194760.1; NC_009976.1.
DR AlphaFoldDB; A9BDE9; -.
DR STRING; 93059.P9211_02041; -.
DR KEGG; pmj:P9211_02041; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_3; -.
DR OrthoDB; 9813612at2; -.
DR Proteomes; UP000000788; 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; 3.90.1150.10; 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; PTHR43643; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR PANTHER; PTHR43643:SF3; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 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:ABX08135.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000788};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ABX08135.1}.
FT DOMAIN 34..362
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 376 AA; 42387 MW; 95A520BC42F46A3E CRC64;
MESFKTSQFV KLPQARQEVE KMTPYSAPLE GRRELLRLDF NENTIGPSPK VIQAIQNIPA
DQISIYPEYN GLKEAIANHL NSSEIANPIK SNQIGLFNGV DAALHAIFHA YGNRKDAFLT
TTPTFGYYHP CACMQGMEII EIPYEQNSFE FPFNRIYKAL IEKNPKLLII CNPNNPTGTN
LSAERIIQLA KASPETLIVI DELYEAFLGD SVIPIVNYEK TPNIVVLRSL SKTYGLAGLR
IGFAIGHMAV VNRIQRVTGP YDINSFAVTA AFAALKDQAY IDEYIREVLR AREWIKTKLK
EHDVRHVIQS GNYFLLWPKS NVSIVEQSLK KHGVLVRNMN NKPLLEGALR VSIGVSTQME
QFWEAFKKSD EVKALA
//
