ID A0A9Q1HA61_HOLLE Unreviewed; 410 AA.
AC A0A9Q1HA61;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE SubName: Full=Hydroxyacid oxidase 1 {ECO:0000313|EMBL:KAJ8041637.1};
GN ORFNames=HOLleu_12510 {ECO:0000313|EMBL:KAJ8041637.1};
OS Holothuria leucospilota (Black long sea cucumber) (Mertensiothuria
OS leucospilota).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Holothuriidae; Holothuria.
OX NCBI_TaxID=206669 {ECO:0000313|EMBL:KAJ8041637.1, ECO:0000313|Proteomes:UP001152320};
RN [1] {ECO:0000313|EMBL:KAJ8041637.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nanhai2018 {ECO:0000313|EMBL:KAJ8041637.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAJ8041637.1};
RA Chen T.;
RT "Tropical sea cucumber genome reveals ecological adaptation and Cuvierian
RT tubules defense mechanism.";
RL Submitted (OCT-2021) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAJ8041637.1}.
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DR EMBL; JAIZAY010000005; KAJ8041637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9Q1HA61; -.
DR OrthoDB; 25826at2759; -.
DR Proteomes; UP001152320; Chromosome 5.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:TreeGrafter.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:TreeGrafter.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IEA:TreeGrafter.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 PANTHER; PTHR10578:SF149; 2-HYDROXYACID OXIDASE 2; 1.
DR PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR Pfam; PF01070; FMN_dh; 2.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000138-2};
KW FMN {ECO:0000256|PIRSR:PIRSR000138-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP001152320}.
FT DOMAIN 2..404
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 28
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 81..83
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 110
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 132
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 134
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 160
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 169
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 240
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 296
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 298
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 301
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 330..334
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 353..354
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 410 AA; 45536 MW; AF3206E4481FD81B CRC64;
MASSSALVCV KAYEQVAREL LSKQAWAYYS AGADEETTLN ECNEAYKRYY LIPRILRPVK
DRDLSTLIQG EPISFPVCVS PTAYHKFANE EGEVATAKAA SSCRTLMILS VISNCRLEDL
ATAAPSGLRW MQTYMFRDKK LVEIIIRRAE RSGYKGLVLT VDDPREGKRY KTLGFGWEGI
YKQEGLGMVN LDVDLEDVKR AKEAGDKNLT NYGYWQTNSY ATWEYVKWIK TITNLPIILK
GINSRKQITD LRLLSVITDK IGENRTVGKL ADLLKAYRAA SVREAVESGI QGILVSVHGG
RQLDCVPPPI EMLPKIVEVT KNTGIEVYID GGIRTGTDVL KALALGARAV FIGRPVLWGL
AVKGQQGVRD VIEILRDEFD RAMALSGCST VNDVDSSLVL YKGDLHNAKL
//
