ID A0A2M8IYW1_9RHOB Unreviewed; 388 AA.
AC A0A2M8IYW1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Alpha-hydroxy-acid oxidizing enzyme {ECO:0000313|EMBL:PJE35678.1};
DE EC=1.1.2.3 {ECO:0000313|EMBL:PJE35678.1};
GN Name=lldD {ECO:0000313|EMBL:PJE35678.1};
GN ORFNames=CVM52_15950 {ECO:0000313|EMBL:PJE35678.1};
OS Pseudooceanicola lipolyticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=2029104 {ECO:0000313|EMBL:PJE35678.1, ECO:0000313|Proteomes:UP000231553};
RN [1] {ECO:0000313|EMBL:PJE35678.1, ECO:0000313|Proteomes:UP000231553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=157 {ECO:0000313|EMBL:PJE35678.1,
RC ECO:0000313|Proteomes:UP000231553};
RX PubMed=29219804; DOI=10.1099/ijsem.0.002521;
RA Huang M.-M., Guo L.-L., Wu Y.-H., Lai Q.-L., Shao Z.-Z., Wang C.-S., Wu M.,
RA Xu X.-W.;
RT "Pseudooceanicola lipolyticus sp. nov., a marine alphaproteobacterium,
RT reclassification of Oceanicola flagellatus as Pseudooceanicola flagellatus
RT comb. nov. and emended description of the genus Pseudooceanicola.";
RL Int. J. Syst. Evol. Microbiol. 68:409-415(2018).
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:PJE35678.1}.
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DR EMBL; PGTB01000077; PJE35678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8IYW1; -.
DR OrthoDB; 9770452at2; -.
DR Proteomes; UP000231553; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004460; F:L-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
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 InterPro; IPR008259; FMN_hydac_DH_AS.
DR PANTHER; PTHR10578:SF107; FMN HYDROXY ACID DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 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|PIRSR:PIRSR000138-2};
KW FMN {ECO:0000256|PIRSR:PIRSR000138-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:PJE35678.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231553}.
FT DOMAIN 1..381
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 276
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 25
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 78..80
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 107
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 128
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 130
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 156
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 165
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 252
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 274
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 276
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 279
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 307..311
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 330..331
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 388 AA; 42344 MW; E615F0F86E24EEFA CRC64;
MPVITTIDDL KRLHERRVPR MFYDYAESGS WTEQTFRDNT SDFARIRLRQ KVAVDMSGRS
TASKMIGQDV AMPVALAPVG LTGMQHADGE IKAAQAAAAF GVPFTLSTMS INSIEDVAEA
TDKPFWFQLY TMKDADYVRR LIERARAAKC SALVITLDLQ ILGQRHKDLK NGLSAPPKLT
PKTVANLLTK WSWGIGMLGA KRRHFGNIVG HVQGVSDTAA LGAWTAEQFD LTLDWNKIAK
LMEMWDGKVI LKGILDPEDA KMAAKLGADA IIVSNHGGRQ LDGALSSIRM LRPILDAVGG
ETEVHLDSGI RSGQDVLKAL AMGAKGTMIG RAFVYGLGAM GRKGVETALS VIHKELDTTM
ALCGETDVND LGRHNLLIPD DFEGRWQA
//