ID A0A6G8Q540_9ACTN Unreviewed; 408 AA.
AC A0A6G8Q540;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 08-OCT-2025, entry version 22.
DE SubName: Full=Alpha-hydroxy-acid oxidizing protein {ECO:0000313|EMBL:QIN81570.1};
GN ORFNames=GBA63_02205 {ECO:0000313|EMBL:QIN81570.1};
OS Rubrobacter tropicus.
OC Bacteria; Bacillati; Actinomycetota; Rubrobacteria; Rubrobacterales;
OC Rubrobacteraceae; Rubrobacter.
OX NCBI_TaxID=2653851 {ECO:0000313|EMBL:QIN81570.1, ECO:0000313|Proteomes:UP000501452};
RN [1] {ECO:0000313|EMBL:QIN81570.1, ECO:0000313|Proteomes:UP000501452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 52909 {ECO:0000313|EMBL:QIN81570.1,
RC ECO:0000313|Proteomes:UP000501452};
RA Chen R.W.;
RT "Rubrobacter sp nov SCSIO 52090 isolated from a deep-sea sediment in the
RT South China Sea.";
RL Submitted (OCT-2019) 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}.
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DR EMBL; CP045119; QIN81570.1; -; Genomic_DNA.
DR RefSeq; WP_166173075.1; NZ_CP045119.1.
DR AlphaFoldDB; A0A6G8Q540; -.
DR KEGG; rub:GBA63_02205; -.
DR Proteomes; UP000501452; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004459; F:L-lactate dehydrogenase (NAD+) activity; IEA:TreeGrafter.
DR GO; GO:0009060; P:aerobic respiration; IEA:TreeGrafter.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR FunFam; 3.20.20.70:FF:000029; L-lactate dehydrogenase; 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 InterPro; IPR008259; FMN_hydac_DH_AS.
DR PANTHER; PTHR10578:SF107; 2-HYDROXYACID OXIDASE 1; 1.
DR PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR000138-
KW 2}; FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRSR:PIRSR000138-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000501452}.
FT DOMAIN 11..392
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 37
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 90..92
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 119
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 140
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 142
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 167
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 176
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 263
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 285
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 287
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 290
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 318..322
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 341..342
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 408 AA; 44547 MW; 26ED8E09D374FC53 CRC64;
MGPFGFDYRL VAPEKLLSLD DYRREAKRRL PKMVWSYVDG GADDHVTISD NREAFGRWSF
RTRVLAGHAA RDLSVKAAGV TLDLPIILGP TGFAGLSYWR GDIAALKAAE RHGTRYAVST
VSSWSIEEIA RESGVDHFFQ LYPQSGELAA SLMRRAWNAG QKTMFVTVDV PVRGNREGER
KHGMGIPPVL TPRRLLNVAR HPKWALDVLL HQRIGGRSLA TTGGVTGAIE SIEIQSRELM
QSTLDWDDLA WMRDKWKGNL YIKGVLDPED ATRAVDLGLD GVVVSNHGGR QLDFTPATLD
VLPDIADAVG DRAEVLMDGG VRRGSDVVKA LALGADAVLI GRPYLYGLAV NGEDGVAHVL
DILREEIDTT LALMGVGSVA ELDRSWIVPR ASAAAQSQNT SAFRDQTV
//
