ID Q0C3Q0_HYPNA Unreviewed; 467 AA.
AC Q0C3Q0;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE SubName: Full=Oxidoreductase, FAD-binding {ECO:0000313|EMBL:ABI75571.1};
GN OrderedLocusNames=HNE_0916 {ECO:0000313|EMBL:ABI75571.1};
OS Hyphomonas neptunium (strain ATCC 15444).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hyphomonas.
OX NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI75571.1, ECO:0000313|Proteomes:UP000001959};
RN [1] {ECO:0000313|EMBL:ABI75571.1, ECO:0000313|Proteomes:UP000001959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI75571.1,
RC ECO:0000313|Proteomes:UP000001959};
RX PubMed=16980487; DOI=10.1128/JB.00111-06;
RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA Ward N.L.;
RT "Comparative genomic evidence for a close relationship between the
RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT crescentus.";
RL J. Bacteriol. 188:6841-6850(2006).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; CP000158; ABI75571.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0C3Q0; -.
DR STRING; 228405.HNE_0916; -.
DR KEGG; hne:HNE_0916; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_4_1_5; -.
DR Proteomes; UP000001959; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 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; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 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 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000001959}.
FT DOMAIN 37..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 467 AA; 48838 MW; 00F1A55219C8F860 CRC64;
MLPSAFLAAV KDLLGPKGWS EAPETLLAAS TPWRGTYQGN TPLIVRPAST TEAAALVKLC
GQYGVAMTPQ GGNTGLIDGG TPHGEVCVSM TRMNALRETD TFNNSLTIEA GATLVAAQQA
AEAAGRLFPL SLGSEGTATI GGLISTNAGG VAVLRYGMMR DLILGLEVVL PSGEVWDGLS
GLRKNNTGYD LKHLFAGAEG TLGLITAATL KLFPQVSSAT AWVICASADD VVKLLSLVRG
RVGDSVTSFE IIPANAVDMV VADIPTARDP MPSNAPWRVL MEVSQTDGAY ARTLLESALA
AAMEEGLVQD AAIATSEAQA KAFWHIRETI PLSKRAYGAA LNQDISVPVS RIPVFIEACN
AAVRTVLPTA DFVIFGHVGD GNLHYSVVEA QGAAAPQLKD HEGAITRVIY DTVMAHGGSI
SAEHGVGRLK RDELARLRPP AATQAMRAIK RALDPQGIMN PGRVVSV
//
