ID   Q7V6V9_PROMM            Unreviewed;       404 AA.
AC   Q7V6V9;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   11-JAN-2011, entry version 45.
DE   SubName: Full=Aminotransferases class-I;
DE            EC=2.6.1.1;
GN   Name=aspC; OrderedLocusNames=PMT_1029;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22825698; 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: Pyridoxal phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family.
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   HSSP; O59096; 1DJU.
DR   ProteinModelPortal; Q7V6V9; -.
DR   SMR; Q7V6V9; 33-391.
DR   STRING; Q7V6V9; -.
DR   GeneID; 1727554; -.
DR   GenomeReviews; BX548175_GR; PMT_1029.
DR   KEGG; pmt:PMT1029; -.
DR   NMPDR; fig|74547.1.peg.1027; -.
DR   eggNOG; COG0436; -.
DR   HOGENOM; HBG320597; -.
DR   OMA; PICASII; -.
DR   ProtClustDB; PRK05957; -.
DR   BioCyc; PMAR74547:PMT1029-MONOMER; -.
DR   GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; IEA:InterPro.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   InterPro; IPR001176; ACC_synthase.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Complete proteome; Pyridoxal phosphate; Transferase.
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
//