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
//