ID I4BYZ3_ACEMN Unreviewed; 337 AA.
AC I4BYZ3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Alpha-hydroxyacid dehydrogenase, FMN-dependent L-lactate dehydrogenase {ECO:0000313|EMBL:AFM22500.1};
GN OrderedLocusNames=Anamo_1914 {ECO:0000313|EMBL:AFM22500.1};
OS Acetomicrobium mobile (strain ATCC BAA-54 / DSM 13181 / JCM 12221 / NGA)
OS (Anaerobaculum mobile).
OC Bacteria; Synergistota; Synergistia; Synergistales; Acetomicrobiaceae;
OC Acetomicrobium.
OX NCBI_TaxID=891968 {ECO:0000313|EMBL:AFM22500.1, ECO:0000313|Proteomes:UP000006061};
RN [1] {ECO:0000313|Proteomes:UP000006061}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-54 / DSM 13181 / NGA
RC {ECO:0000313|Proteomes:UP000006061};
RX PubMed=23961311; DOI=10.4056/sigs.3547050;
RA Mavromatis K., Stackebrandt E., Held B., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Land M., Rohde M., Spring S., Goker M., Woyke T.,
RA Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of the moderate thermophile Anaerobaculum mobile
RT type strain (NGA(T)).";
RL Stand. Genomic Sci. 8:47-57(2013).
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; CP003198; AFM22500.1; -; Genomic_DNA.
DR AlphaFoldDB; I4BYZ3; -.
DR STRING; 891968.Anamo_1914; -.
DR KEGG; amo:Anamo_1914; -.
DR PATRIC; fig|891968.3.peg.1899; -.
DR eggNOG; COG1304; Bacteria.
DR HOGENOM; CLU_020639_6_0_0; -.
DR Proteomes; UP000006061; Chromosome.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
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; IPR001295; Dihydroorotate_DH_CS.
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; 2.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 2.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS00912; DHODEHASE_2; 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:UP000006061}.
FT DOMAIN 38..337
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51349"
FT ACT_SITE 235
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT BINDING 88..90
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 211
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 233
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 235
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 238
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 266..270
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT BINDING 289..290
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ SEQUENCE 337 AA; 35331 MW; D1FCEE94B188D027 CRC64;
MLRWEDVLER ARESLKGICH LCPVCDMKAC AGKVPGIGGI GTGSSAKNNY EALRGLKFKM
KLLHDVDKPD MGVELFGQKL ALPVIGAAVA GAKVNFAAKI AEKEFAQAQL VGAMEAGTIA
MIGDGPGDLY DDTVAALREA GKGIAIIKPR EFDEIMRRIK MAEEAGALAV GIDVDAAGLV
NMRRSGELVR PLNPNILKRI CESSNLPVIV KGIMAEEEAV MACDAGASAI VVSNHGGRVL
DDLPGTISVL PGIASRVRGR CIVLADGGVR TGSDVLKFLA CGASAVLVGR PVVWGVFGGG
KEGVRLLYER LAQELSVAMM LTSCPSVREV SHCISGN
//
