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Database: UniProt
Entry: A0A0M2UQJ8_9BACT
LinkDB: A0A0M2UQJ8_9BACT
Original site: A0A0M2UQJ8_9BACT 
ID   A0A0M2UQJ8_9BACT        Unreviewed;       498 AA.
AC   A0A0M2UQJ8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Putative D-lactate dehydrogenase {ECO:0000313|EMBL:KKO18373.1};
GN   ORFNames=BROFUL_02937 {ECO:0000313|EMBL:KKO18373.1};
OS   Candidatus Brocadia fulgida.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Brocadia.
OX   NCBI_TaxID=380242 {ECO:0000313|EMBL:KKO18373.1, ECO:0000313|Proteomes:UP000034954};
RN   [1] {ECO:0000313|EMBL:KKO18373.1, ECO:0000313|Proteomes:UP000034954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU1 {ECO:0000313|EMBL:KKO18373.1};
RX   PubMed=24267221; DOI=10.1186/1471-2180-13-265;
RA   Ferousi C., Speth D.R., Reimann J., Op den Camp H.J., Allen J.W.,
RA   Keltjens J.T., Jetten M.S.;
RT   "Identification of the type II cytochrome c maturation pathway in anammox
RT   bacteria by comparative genomics.";
RL   BMC Microbiol. 13:265-265(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KKO18373.1}.
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DR   EMBL; LAQJ01000276; KKO18373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2UQJ8; -.
DR   Proteomes; UP000034954; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000034954}.
FT   DOMAIN          21..236
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   498 AA;  55234 MW;  6BEACFB2779B71FC CRC64;
     MIRSADPDAI RPYLKDASNL SGGYADEVVF PEDEKEVAGI LEEASSTKTP VTIAGNGTGL
     VGARIPFGGI VLSTEKLGGL RHIHQAAGEP GYAVTGPAIT LRALQEAVSA KGLLYPPDPT
     EQNAFLGATV ATNASGARTF KYGATRRWIR RLKVVLATGD ILELQRGECL ADKEGRLFLT
     GSRNVLQLKL PQYRMPEGKH SAGYYVAPGM SALDLFIGSE GTLGVITEIE LALIPQPREL
     FSGIIFFGRE EDAWQFANQA RNESLKNRAL QIKNQIDASA LEYFDAHSLD ALRSAYSQIP
     SKAQSAIFFE QEIQPDFGKL LREQWGRLCI DHQALSDQSW FSRSAQEHTE FRAFRHAIPV
     LVNRILRQHQ QTKIGTDFTV PHEHLFGLFK LYRQSLCDAG LRYCIFGHVA DNHLHVNLLP
     RNDQEADRGW AIYRKIAQQV IAWGGTISAE HGVGKIKREY LLDMFGQLGL REMAAMKKKL
     DPCLILGRGN IIPEEFLL
//
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