FLAV_HELPJ
ID FLAV_HELPJ Reviewed; 164 AA.
AC Q9ZK53;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Flavodoxin;
GN Name=fldA; OrderedLocusNames=jhp_1088;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
CC -!- FUNCTION: Low-potential electron donor to a number of redox enzymes.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the flavodoxin family. {ECO:0000305}.
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DR EMBL; AE001439; AAD06670.1; -; Genomic_DNA.
DR PIR; H71850; H71850.
DR RefSeq; WP_000516049.1; NZ_CP011330.1.
DR PDB; 1FUE; X-ray; 2.40 A; A=2-164.
DR PDBsum; 1FUE; -.
DR AlphaFoldDB; Q9ZK53; -.
DR SMR; Q9ZK53; -.
DR STRING; 85963.jhp_1088; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR EnsemblBacteria; AAD06670; AAD06670; jhp_1088.
DR KEGG; hpj:jhp_1088; -.
DR PATRIC; fig|85963.30.peg.1494; -.
DR eggNOG; COG0716; Bacteria.
DR OMA; ICGIPTW; -.
DR EvolutionaryTrace; Q9ZK53; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR010086; Flavodoxin_lc.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR PIRSF; PIRSF038996; FldA; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR TIGRFAMs; TIGR01752; flav_long; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Flavoprotein; FMN; Transport.
FT CHAIN 1..164
FT /note="Flavodoxin"
FT /id="PRO_0000171635"
FT DOMAIN 4..160
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1FUE"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1FUE"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:1FUE"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1FUE"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1FUE"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:1FUE"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:1FUE"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1FUE"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:1FUE"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:1FUE"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:1FUE"
FT TURN 89..93
FT /evidence="ECO:0007829|PDB:1FUE"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:1FUE"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1FUE"
FT STRAND 129..139
FT /evidence="ECO:0007829|PDB:1FUE"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1FUE"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1FUE"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:1FUE"
SQ SEQUENCE 164 AA; 17473 MW; 19CCF277135776D6 CRC64;
MGKIGIFFGT DSGNAEAIAE KISKAIGNAE VIDVAKASKE QFNGFTKVIL VAPTAGAGDL
QTDWEDFLGT LEASDFANKT IGLVGLGDQD TYSETFAEGI FHIYEKAKAG KVVGQTPTDG
YHFEASKAVE GGKFVGLVID EDNQDDLTDE RIAKWVEQVK GSFA
