ID A0A2S6NL54_RHOGL Unreviewed; 394 AA.
AC A0A2S6NL54;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Alpha-hydroxy-acid oxidizing enzyme {ECO:0000313|EMBL:PPQ35973.1};
GN ORFNames=CCS01_06180 {ECO:0000313|EMBL:PPQ35973.1};
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ35973.1, ECO:0000313|Proteomes:UP000239724};
RN [1] {ECO:0000313|EMBL:PPQ35973.1, ECO:0000313|Proteomes:UP000239724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ35973.1,
RC ECO:0000313|Proteomes:UP000239724};
RX PubMed=29423563;
RA Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT "New insights into the metabolic potential of the phototrophic purple
RT bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT and evidence for a vanadium-dependent nitrogenase.";
RL Arch. Microbiol. 0:0-0(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:PPQ35973.1}.
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DR EMBL; NHRY01000064; PPQ35973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6NL54; -.
DR OrthoDB; 9770452at2; -.
DR Proteomes; UP000239724; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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: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; 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:UP000239724}.
FT DOMAIN 2..387
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 282
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 81..83
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 131
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 133
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 159
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 168
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 258
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 280
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 282
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 285
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 313..317
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 336..337
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 394 AA; 43754 MW; E11E03DF52F9A097 CRC64;
MAALDHCYNV FDLREAARRR LPRGVFEFVD RATEDELALR NNRAAFEKIK LLHRALVDVS
GRATTTTLFG KEIALPMAIA PTGAAGLCWH EGELELAKAA ARAKIPFTLA TGAMTAMEKI
AKEANFRLWF QLYVWKRREL SYQLIERAKA NGFEALIVTT DTIVSPNREY NAKNGFLLPF
HPTWRFTWDI MQHPTWFGTV LLKYFTTIGM PRNENYPDPY RRPVTSDAST QEVMRQDSLC
WDDIRIFRDK WPGILMLKGI NRVDDALKAI SYGVDGLIVS NHGGRNMDSA AATIDILPDI
AQAVGDKATV ILDSGVRRGS DIVKAVALGA KCVLTGRATL YGTAVGGEAG AAKAVSIIRG
EMDKTMAYTG CNRVDEITPD IFFASRDSNR LVAE
//
