ID A0A254Q9P9_9BURK Unreviewed; 969 AA.
AC A0A254Q9P9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:OWS72242.1};
GN ORFNames=CBI30_03370 {ECO:0000313|EMBL:OWS72242.1};
OS Polynucleobacter aenigmaticus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=1743164 {ECO:0000313|EMBL:OWS72242.1, ECO:0000313|Proteomes:UP000198104};
RN [1] {ECO:0000313|EMBL:OWS72242.1, ECO:0000313|Proteomes:UP000198104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-K35W1 {ECO:0000313|EMBL:OWS72242.1,
RC ECO:0000313|Proteomes:UP000198104};
RA Hahn M.W.;
RT "Polynucleobacter sp. MWH-K35W1 isolated from the permanently anoxic
RT monimolimnion of a meromictic lake.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OWS72242.1}.
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DR EMBL; NGUO01000004; OWS72242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254Q9P9; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000198104; 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; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR004017; Cys_rich_dom.
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:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02754; CCG; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT DOMAIN 39..267
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 969 AA; 106297 MW; 47E710A0B65E4E56 CRC64;
MGSISQWEQL NVELTAALGS SVHFDTAHQA VYASEASNYR QIPIGVVTPK NTEEFIKGIE
ICHRNKAPVL MRGAGTSMNG QTVNNAVVFD ISKYCNHILA LDPVAGNALV EPGVICDSLR
DAAELHGLTF APDPSTHSRC TLGGMVANNS CGAHSVMAGK TLENTEALEI LTYDGERFWV
GPTSDQELAQ IIAAGGRRGQ IYQDLLTLRD RYADLIRARF PNIKRRVSGY NLDQLLPENG
FNVAKALVGT EGTCALTLAA KVRLVKSPAK RVVLVLGFED IYVAGDAVPE YQSFNPIAIE
GLDYKIIRGL QQRNLAKAEI DLLPPGNAWV VVEFGDDTLE GAVAQAEKAQ QYFKARTKGP
QPSTWLVPDP LVQKRIWSIR ENGASATHLS IDPNSPDPVV GWEDAAVDPA RLGEYLRAFQ
ALVDSYEYET SLYGHFGDGC IHARITFNLR SAEGVAKFRS FIRDAATLVV AFGGSLTGEH
GDGQARAEFL PIMFGEELMG AMHEFKRIWD PQNKLNPGKV VHPYRVDENL RMGPEYKVVN
IKTRLNFLSQ EGNGFQRAVE RCVGMGKCRS EKVGTMCPSY RATKEERFST RGRSRLFWEM
LQGEVIKDGW ESNELKEALD TCLSCKGCKS DCPAHVDMAS YKAEFLSHYH ETNSRPRQAL
TMGRIGDWAP LASKFSWLIN GVMQTPVLSS IAKWVGGVAQ ERSLPKFASQ SFRKQFKQST
NASVGQKKVI LWVDTFCEHF HPEVANAAVE VLAHAGFEAT LPKTPLCCGR PLYDFGYLDL
AKQKLEKILD AIGDQIGAGD DSPIAVVGLE PGCMSVFKDE LLKFFPHDPR AKLLSSSSYL
LGDFLHEQGY VPPPLDCNVL VHSHCHQKSL FGTKGDVALL SALGAKADYI DSGCCGMAGS
FGFNPEHVEL SKAVGELVLL PAIRSADQET IILTNGFSCR EQIEQETGRK VKHLAELLQM
AHQQAAKAS
//