ID A0A0P7YCI6_9RHOB Unreviewed; 485 AA.
AC A0A0P7YCI6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=CDP-4-dehydro-6-deoxyglucose reductase {ECO:0000313|EMBL:KPP85919.1};
DE EC=1.17.1.1 {ECO:0000313|EMBL:KPP85919.1};
GN Name=ascD {ECO:0000313|EMBL:KPP85919.1};
GN ORFNames=HLUCCO07_03760 {ECO:0000313|EMBL:KPP85919.1};
OS Rhodobacteraceae bacterium HLUCCO07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666914 {ECO:0000313|EMBL:KPP85919.1, ECO:0000313|Proteomes:UP000050369};
RN [1] {ECO:0000313|EMBL:KPP85919.1, ECO:0000313|Proteomes:UP000050369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO07 {ECO:0000313|EMBL:KPP85919.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KPP85919.1}.
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DR EMBL; LJSU01000018; KPP85919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7YCI6; -.
DR STRING; 1666914.HLUCCO07_03760; -.
DR PATRIC; fig|1666914.4.peg.1692; -.
DR Proteomes; UP000050369; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047099; F:CDP-4-dehydro-6-deoxyglucose reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KPP85919.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..317
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 485 AA; 51905 MW; 9E52D39A9D6ECB3E CRC64;
MTQKAEVTPG AAWPALPARA MALVYLVACL LPIGIGALSR AAPLDPWEAF GAGLGLAGLT
AMAVQVLTSG RFRAVSGGMG IDRVMAFHKI AAYVVVLMLV LHPLAYVWPT WLDDPARGSE
RLVAYLTGPD WRSGVIALGA LVLLVVMGVA RDVFRYEIWR GSHVILALVA LGGGLHHAAS
AGRLSALGAL HGFWWAVGAV IVLAFAVLYG WRWLRLHRQP WELRSVEPKA DRVWELDIQP
AEGTAPVVYR AGQFVWMTVA GRRFPLFDHP FSIADSPRRA GLSLIIKEAG DFTSTVGDLR
PGTAIGIDGP YGTFTLERHS GDHVLLVAGG VGIAPIMGLL RDLVARGNTR PVRLAYAVGQ
PENFACLDEI EAARAVLDLD VLLISESGEG WDGATGYLDR AKLEAILGGL APERGVALMC
GPGPMVTKVS DTLEDMGMPW RNVVYERFDY AGGLSARQDR RRTLGFVGVF AALAGLVAAL
SQIVL
//
