ID Q7V6V9_PROMM Unreviewed; 404 AA. AC Q7V6V9; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 07-JAN-2015, entry version 69. DE SubName: Full=Aminotransferases class-I {ECO:0000313|EMBL:CAE21204.1}; DE EC=2.6.1.1 {ECO:0000313|EMBL:CAE21204.1}; GN Name=aspC {ECO:0000313|EMBL:CAE21204.1}; GN OrderedLocusNames=PMT_1029 {ECO:0000313|EMBL:CAE21204.1}; OS Prochlorococcus marinus (strain MIT 9313). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=74547 {ECO:0000313|EMBL:CAE21204.1, ECO:0000313|Proteomes:UP000001423}; RN [1] {ECO:0000313|EMBL:CAE21204.1, ECO:0000313|Proteomes:UP000001423} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9313 {ECO:0000313|Proteomes:UP000001423}; RX PubMed=12917642; DOI=10.1038/nature01947; RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., RA Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., RA Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., RA Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A., RA Webb E.A., Zinser E.R., Chisholm S.W.; RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic RT niche differentiation."; RL Nature 424:1042-1047(2003). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|RuleBase:RU000479}; CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|RuleBase:RU000479}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX548175; CAE21204.1; -; Genomic_DNA. DR RefSeq; NP_894860.1; NC_005071.1. DR ProteinModelPortal; Q7V6V9; -. DR STRING; 74547.PMT1029; -. DR EnsemblBacteria; CAE21204; CAE21204; PMT_1029. DR GeneID; 1727554; -. DR KEGG; pmt:PMT1029; -. DR PATRIC; 23010377; VBIProMar135351_1339. DR eggNOG; COG0436; -. DR OMA; DEAYEDF; -. DR OrthoDB; EOG6RRKNS; -. DR Proteomes; UP000001423; Chromosome. DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 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_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000256|RuleBase:RU000481, KW ECO:0000313|EMBL:CAE21204.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000001423}; KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000479}; KW Reference proteome {ECO:0000313|Proteomes:UP000001423}; KW Transferase {ECO:0000256|RuleBase:RU000481, KW ECO:0000313|EMBL:CAE21204.1}. SQ SEQUENCE 404 AA; 43966 MW; 486617E2F7B8C836 CRC64; MNSFSSSKHP QPGTQIDAVL DPVIPALNEL VAKTPGTLSL AQGMVNWPPP IAVKLAMNNA LLNQESSLNR YGPARGDPDL LELIKQKLMM QNGLDLAESM VMVTAGSNMA FHAIAQVLCD PGDEVILPLP YYFNHFMAIQ LAGGVPVPVN AGLIPNPGLI EAAITKRTRA IVTISPNNPS GIVFPQTLLA AINRICAQHG LLHISDEAYE DFVFGDVPHW SPGSLPGAGN HTVSLYSFSK AYGMAGWRLG YMSVPIVWSK ALEKVQDTVL ICPPRFCQRA AIAALLDGSD WVRQNVSQLM SRYQLLLKRF AASNDRPWRF LHEPNGAFYC LLEVDCGCNG DTLMRQLVRD YRVATIGGCS FGFKNESCVL RISVGMLEGA ELIDAFNRLE AGMLNAVQQG DRTT //