putative citrate synthase [Klebsiella pneumoniae subsp. pneumoniae

LOCUS       YP_005225597             434 aa            linear   CON 02-JUN-2020
            HS11286].
ACCESSION   YP_005225597
VERSION     YP_005225597.1
DBLINK      BioProject: PRJNA84387
            Assembly: GCF_000240185.1
DBSOURCE    REFSEQ: accession NC_016845.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae subsp. pneumoniae HS11286
  ORGANISM  Klebsiella pneumoniae subsp. pneumoniae HS11286
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group;
            Klebsiella; Klebsiella pneumoniae complex.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Liu,P., Li,P., Jiang,X., Bi,D., Xie,Y., Tai,C., Deng,Z.,
            Rajakumar,K. and Ou,H.Y.
  TITLE     Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae
            HS11286, a multidrug-resistant strain isolated from human sputum
  JOURNAL   J. Bacteriol. 194 (7), 1841-1842 (2012)
   PUBMED   22408243
REFERENCE   2  (residues 1 to 434)
  CONSRTM   NCBI Genome Project
  TITLE     Direct Submission
  JOURNAL   Submitted (06-FEB-2012) National Center for Biotechnology
            Information, NIH, Bethesda, MD 20894, USA
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Ou,H.-Y., Jiang,X., Liu,P. and Li,P.
  TITLE     Direct Submission
  JOURNAL   Submitted (14-DEC-2011) State Key Laboratory of Microbial
            Metabolism, Shanghai Jiaotong University, 1954 Huashan Road,
            Shanghai 200030, China
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence is identical to AEW59995.
            RefSeq Category: Reference Genome
                        CLI: Clinical Isolate
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Klebsiella pneumoniae subsp. pneumoniae
                     HS11286"
                     /strain="HS11286"
                     /sub_species="pneumoniae"
                     /db_xref="taxon:1125630"
     Protein         1..434
                     /product="putative citrate synthase"
                     /calculated_mol_wt=47807
     Region          19..416
                     /region_name="EcCS_like"
                     /note="Escherichia coli (Ec) citrate synthase (CS)
                     GltA_like. CS catalyzes the condensation of acetyl
                     coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate
                     and coenzyme A (CoA), the first step in the citric acid
                     cycle (TCA or Krebs cycle). The overall CS...; cd06114"
                     /db_xref="CDD:99867"
     Site            order(41..57,59,71..74,77,81,86,94..97,99,102..103,
                     106..107,118,121..122,124..126,130,134,138,141,144..146,
                     231..235,238..239,243,246..249,252,259..260,262..267,
                     269..270,308..309,406,408..416)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99867"
     Site            order(49,231,234,265..267,269,272,301..308,311,316,357,
                     359,362,364,385,389,406,409)
                     /site_type="active"
                     /db_xref="CDD:99867"
     Site            order(49,231,234,265..266,301..302,304..308,316,362,389)
                     /site_type="other"
                     /note="citrylCoA binding site [chemical binding]"
                     /db_xref="CDD:99867"
     Site            order(108,110..116,147,165,169,191)
                     /site_type="other"
                     /note="NADH binding [chemical binding]"
                     /db_xref="CDD:99867"
     Site            order(113..121,124..129,180..192,206..207)
                     /site_type="active"
                     /note="cationic pore residues [active]"
                     /db_xref="CDD:99867"
     Site            order(231,234,266..267,307,316,364,385,389,409)
                     /site_type="other"
                     /note="oxalacetate/citrate binding site [chemical
                     binding]"
                     /db_xref="CDD:99867"
     Site            order(265..266,269,272,301..306,308,311,357,359,362,364,
                     406)
                     /site_type="other"
                     /note="coenzyme A binding site [chemical binding]"
                     /db_xref="CDD:99867"
     Site            order(266,307,364)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:99867"
     CDS             1..434
                     /locus_tag="KPHS_12970"
                     /coded_by="NC_016845.1:1341074..1342378"
                     /transl_table=11
                     /db_xref="GeneID:11846298"
CONTIG      join(WP_004198770.1:1..434)
ORIGIN      
        1 msttpltlsf agqqpplalp qvpgtrgpvg vdmrgldqsg fcsydpgfan tagcqsaisw
       61 idtensvllh rgypvdqlar qcdflevayi mlngdapdea syqtfretit rhtlvheqia
      121 rmcsgfrrds hpmalmcalv galaafyhdv ldvenpqhra laatrllskm ptiaamsyky
      181 tieqpaaypr ndlsyagnfl qmlfaipaek yvlnpvieqa mnqilvlhad hgqcastttv
      241 raagssganl facvaaglas lwgpmhggan essmrmleei esvdqvpafl rqakrdpqaf
      301 rrlgfgnsry rhrdpradil retshrvlae vgmsdrllqv amaledvalt dpyfvdngls
      361 psvdfytavi lkamnlpssm favvtavgrt vgwvahwnem hqapltiyrp rqiyvgegyr
      421 dyvsrrgers aelr