LOCUS       BAQ45834.1               430 aa    PRT              BCT 16-MAY-2017
DEFINITION  Methylobacterium aquaticum type II citrate synthase protein.
ACCESSION   AP014704-2414
PROTEIN_ID  BAQ45834.1
SOURCE      Methylobacterium aquaticum
  ORGANISM  Methylobacterium aquaticum
            Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
            Methylobacteriaceae; Methylobacterium.
REFERENCE   1  (bases 1 to 5348274)
  AUTHORS   Tani,A. and Ogura,Y.
  TITLE     Direct Submission
  JOURNAL   Submitted (21-JAN-2015) to the DDBJ/EMBL/GenBank databases.
            Contact:Akio Tani
            Okayama University, Institute of Plant Science and Resources; Chuo
            2-20-1, Kurashiki, Okayama 710-0046, Japan
REFERENCE   2
  AUTHORS   Tani,A., Ogura,Y., Hayashi,T. and Kimbara,K.
  TITLE     Complete Genome Sequence of Methylobacterium aquaticum Strain 22A,
            Isolated from Racomitrium japonicum Moss
  JOURNAL   Genome Announc 3, e00266-15 (2015)
  REMARK    Publication Status: Online-Only
            DOI:10.1128/genomeA.00266-15
COMMENT     ##Genome-Assembly-Data-START##
            Assembly Method       :: Newbler v. 2.7
            Genome Coverage       :: 47x
            Sequencing Technology :: 454 GS FLX; ABI 3730; Illumina PE
            ##Genome-Assembly-Data-END##
FEATURES             Qualifiers
     source          /culture_collection="NBRC:FERM BP-11078"
                     /db_xref="taxon:270351"
                     /mol_type="genomic DNA"
                     /organism="Methylobacterium aquaticum"
                     /strain="MA-22A"
     protein         /EC_number="2.3.3.1"
                     /gene="gltA"
                     /inference="similar to AA sequence:RefSeq:WP_015928212.1"
                     /locus_tag="Maq22A_c13015"
                     /note="257d0002"
                     /note="type II enzyme; in Escherichia coli this enzyme
                     forms a trimer of dimers which is allosterically inhibited
                     by NADH and competitively inhibited by
                     alpha-ketoglutarate; allosteric inhibition is lost when
                     Cys206 is chemically modified which also affects hexamer
                     formation; forms oxaloacetate and acetyl-CoA and water
                     from citrate and coenzyme A; functions in TCA cycle,
                     glyoxylate cycle and respiration; enzyme from Helicobacter
                     pylori is not inhibited by NADH; Derived by automated
                     computational analysis using gene prediction method:
                     Protein Homology."
                     /transl_table=11
BEGIN
        1 MSLPTSTLTV NGRTIELPTK AGTVGPGVVD ISKLYAQTGQ FTYDPGFTST ASCESKITYI
       61 DGDEGVLLYR GYPIEQLAEH GDFLETCYLL LYGELPTAAQ KADFDYRVTR HTMVHDQMNR
      121 FFQGFRRDAH PMAVMVACVG ALSAFYHDST DITDEKQRMV ASMRMIAKMP TLAAMAYKYS
      181 IGQPFVYPKN DLDYTSNFLR MCFAVPCEEY QPNPVLSRAL DRIFILHADH EQNASTSTVR
      241 LAGSSGANPF ACIAAGIACL WGPAHGGANE AALKMLAEIG TPERVGEYVA KAKDKNDPFR
      301 LMGFGHRVYK NYDPRARIMQ KTTHEVLSEL GIKDDPLLDV AMELEQIALK DEYFIEKKLY
      361 PNIDFYSGIT LKAMGFPTSM FTVLFALART VGWISQWAEM IEDPSQKIGR PRQLYTGAPK
      421 RDYVTTAQRG
//