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Database: UniProt
Entry: A0A401ZGB4_9CHLR
LinkDB: A0A401ZGB4_9CHLR
Original site: A0A401ZGB4_9CHLR 
ID   A0A401ZGB4_9CHLR        Unreviewed;       395 AA.
AC   A0A401ZGB4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:GCE05889.1};
GN   ORFNames=KDAU_32180 {ECO:0000313|EMBL:GCE05889.1};
OS   Dictyobacter aurantiacus.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Dictyobacteraceae; Dictyobacter.
OX   NCBI_TaxID=1936993 {ECO:0000313|EMBL:GCE05889.1, ECO:0000313|Proteomes:UP000287224};
RN   [1] {ECO:0000313|Proteomes:UP000287224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S-27 {ECO:0000313|Proteomes:UP000287224};
RA   Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA   Yabe S.;
RT   "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT   sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT   of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT   from Tengu-no-mugimeshi.";
RL   Submitted (DEC-2018) 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:GCE05889.1}.
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DR   EMBL; BIFQ01000001; GCE05889.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401ZGB4; -.
DR   OrthoDB; 9770452at2; -.
DR   Proteomes; UP000287224; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:SF143; DEPENDENT DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G00500)-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000287224}.
FT   DOMAIN          27..393
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   ACT_SITE        288
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-1"
FT   BINDING         53
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         103..105
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         132
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         154
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         156
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         182
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         191
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         264
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         286
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         288
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         291
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         319..323
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
FT   BINDING         342..343
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000138-2"
SQ   SEQUENCE   395 AA;  42930 MW;  CF95B6038CEEEA92 CRC64;
     MKDDQQSIPS YGLGRQMQVY MQGLQGQLPS LPVSPEVLEQ QALAHLSQQA AGYLAGMDDT
     MQANLRAFQR WSILPRMLRD VSRRQLSTTI LGMQLPIPLL LAPIGVQSII HPEAELAVAR
     AARATGVPMI LSTAASRSIE AVAQELADTP RWFQLYWSKN PDLNASLVHR AEQAGYSAIV
     VTLDTRLLSW REQDIQNAYL PFLQGEGLAN YFSDPVFRQA LAQSPEKDPA MAIRYFIDIF
     LNPSLTWDQL AFLRQHTSLP IFLKGVLHPD DARQTIDAGM DGIIVSNHGG RQVGGSRAAL
     DALPAVVEAA GGQVPVLFDS GIRRGSDVLK AIALGARAVL LGRPYIWGLA LDGEAGVQQV
     LQNLLADLDL TLAVSGFSSI SQLDASLLVN ERPTA
//
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