ID   C3ZKZ9_BRAFL            Unreviewed;      1115 AA.
AC   C3ZKZ9;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=FMN hydroxy acid dehydrogenase domain-containing protein {ECO:0000259|PROSITE:PS51349};
GN   ORFNames=BRAFLDRAFT_125550 {ECO:0000313|EMBL:EEN46681.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN46681.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN46681.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN46681.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00024042}.
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DR   EMBL; GG666640; EEN46681.1; -; Genomic_DNA.
DR   RefSeq; XP_002590670.1; XM_002590624.1.
DR   AlphaFoldDB; C3ZKZ9; -.
DR   STRING; 7739.C3ZKZ9; -.
DR   eggNOG; KOG0538; Eukaryota.
DR   eggNOG; KOG2408; Eukaryota.
DR   InParanoid; C3ZKZ9; -.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR   CDD; cd09823; peroxinectin_like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   PANTHER; PTHR11475:SF4; LD42267P; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF01070; FMN_dh; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2}.
FT   DOMAIN          1..358
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   BINDING         855
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ   SEQUENCE   1115 AA;  123309 MW;  A1E25B36A8A10B85 CRC64;
     MSVATLTSIA DFEKSAQEKL LDYVWSYYSK TAGTGQTYQD NLEAFRRYRL IPRNLRDVSI
     RDTSVTVLGT KLDIPVAIAP TAIHRFAHPD AELATAKGAA AMNTGMVLSS WSTRSLEEVA
     EAAPGGVHWF YMLFFNDRGY VKRQLERAER AGYSAIFLTI DQPLFPKPGA SPRSYPFTVR
     FPNIFETDPP HAFGTAEYRQ SLLELVKEYA TWEDVEWVVA NTRLPVVLKG VLSGEDAKMA
     VDRGVKGIYV SNHGGRELDG VPATIDVLPH IVRAVDGKAE VYLDGGVRTG TDVLKALALG
     ARCVFIGRPA LWGLAHNGAE GVQQVLQILT EELSQAMARA GTYFENITTS YFFNESLVVT
     LIKQRNVSKK EEQCTRGDLV TIRLLLILVG LVAIAMAQVS ERELEAAVAR ATLSVDRAIQ
     EEEDLFVAAS DDDARVSPAG RLLAMFRKSK PEARPIARSA EILEDVTSQL TRTGQTDDDF
     SAASDSAATR RVCTNTELRA IRCPQPDPAV REFRSVDGRC NNLDNPLWGA AIQPMKRLLR
     PQYADSVQAP RVRGRGGAAL PSAREVSFTL HEDMRTTSTV NTHLVMQWGQ FLDHDITHTP
     VASAYGGGLI ACPCGSPDRR CFNIPIPSND PDFGGHSCME FVRSSPAPNP GCRVGRRQQL
     DQITAFIDAS MVYGSSEEEL EHLRDPSLGL GQLKSKSNPG DSSKKELLPS AITEEFHCPE
     SSNPSSRNQP CFQAGDVRVN EQPALTSMHT VWLREHNRIA ARLADINSHW DEDRVFYETR
     KIVGAMIQQI TYAEDLPIVL GLNAMNEQCR NQSPIHSLIQ YGLVLRRNGY YSGYDETVDP
     TISNVFATAA YRFGHSLVKS QFERSTSSYN HNAHSPVQLT HSFFNPQHVY NNVQGGLDSI
     VRGLASTPHE KFDRFIVSGL TKNLFADPAG SLGLDLAALN IQRGRDHGLP GYNAWRVLCG
     LPRARSFDDL ATEIPDASTR AKLADLYSHV DDIDLFAAGL AERSVPGGLL GPTFTCLIGR
     QFRELRKGDR FWFENQGQFS QRQLGEVRKV TLARVLCDNT DDTSSMQRHV FELPGPGNQR
     VSCASIPQMD LSAWRESATV VGQVRDFFTD YELVN
//