LOCUS       CDQ48729.1               364 aa    PRT              BCT 04-FEB-2016
DEFINITION  Vibrio anguillarum Putative flavohemoprotein protein.
ACCESSION   LK021129-832
PROTEIN_ID  CDQ48729.1
SOURCE      Vibrio anguillarum
  ORGANISM  Vibrio anguillarum
            Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
            Vibrionaceae; Vibrio.
REFERENCE   1  (bases 1 to 1187342)
  AUTHORS   Holm K.
  JOURNAL   Submitted (26-MAR-2014) to the INSDC. Norstruct, Dept of Chemistry,
            University of Tromso, Science Park 3, NO-9037 Tromso, NORWAY.
REFERENCE   2
  AUTHORS   Holm K.O., Nilsson K., Hjerde E., Willassen N.P., Milton D.L.
  TITLE     Complete genome sequence of Vibrio anguillarum strain NB10, a
            virulent isolate from the Gulf of Bothnia
  JOURNAL   Stand Genomic Sci 10, 60-60(2015).
   PUBMED   26380645
FEATURES             Qualifiers
     source          /organism="Vibrio anguillarum"
                     /chromosome="2"
                     /host="Rainbow trout"
                     /strain="NB10"
                     /mol_type="genomic DNA"
                     /geo_loc_name="Sweden:Baltic Sea, Norrbyn Umeaa"
                     /isolation_source="clinical isolate, Rainbow trout"
                     /serovar="O1"
                     /db_xref="taxon:55601"
     protein         /transl_table=11
                     /gene="hmp"
                     /gene_synonym="fsrB"
                     /gene_synonym="hmpA"
                     /locus_tag="VANGNB10_cII0832c"
                     /old_locus_tag="TVA2386"
                     /function="Is involved in NO detoxification in an aerobic
                     process, termed nitric oxide dioxygenase (NOD) reaction
                     that utilizes O2 and NAD(P)H to convert NO to
                     nitrate,which protects the bacterium from various noxious
                     nitrogen compounds. Therefore, plays a central role in the
                     inducible response to nitrosative stress. In the presence
                     of oxygen and NADH, HMP has NADH oxidase activity, which
                     leads to the generation of superoxide and H2O2, both in
                     vitro and in vivo, and it has been suggested that HMP
                     might act as an amplifier of superoxide stress. Under
                     anaerobic conditions,HMP also exhibits nitric oxide
                     reductase and FAD reductase activities. However, all these
                     reactions are much lower than NOD activity. Various
                     electron acceptors are also reduced by HMP in vitro,
                     including dihydropterine,ferrisiderophores, ferric
                     citrate, cytochrome c, nitrite,S-nitrosoglutathione, and
                     alkylhydroperoxides. However, it is unknown if these
                     reactions are of any biological significance in vivo."
                     /EC_number="1.14.12.17"
                     /note="user locus_tag: VANGcII0832c"
                     /note="ref: P24232 (HMP_ECOLI)"
BEGIN
        1 MFTHNPELKD IFNMTHQHTG RQGVALFEAI AAYAKNIENL AALTSAVERI AQKHTSFNIQ
       61 PEHYQIVGHH LIETLRELAA DAFTPDVEAA WTAAYLFLAQ VFIDREGELY LQRKQAIGGW
      121 ENAREFVLQD KVKESEFVTS FIFEPADGKA VLDYQVGQYI GIELKPEGAS YSEIRQYSLS
      181 QKPNGKNYRI SVKREGVDTE HPGTVSNYLH DYVEKGSRVK LYAPAGDFFY VEKLAPVVLI
      241 SAGVGATPMQ AILQQLASVG KKEVTYLHAC NNLSQHSFID ETATLMAVHP SWQQVVWYLE
      301 SEQTPAKQGS MILHEVCEQL PLTQGDFYIC GPVGFMQFIV EQLELLGVAR ERIHYEVFGP
      361 HAYL
//