ID C6SDA0_NEIME Unreviewed; 455 AA.
AC C6SDA0;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:CBA06850.1};
GN ORFNames=NME_1268 {ECO:0000313|EMBL:CBA06850.1};
OS Neisseria meningitidis alpha153.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=663926 {ECO:0000313|EMBL:CBA06850.1};
RN [1] {ECO:0000313|EMBL:CBA06850.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Alpha153 {ECO:0000313|EMBL:CBA06850.1};
RX PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA Linke B., Vogel U., Frosch M.;
RT "Whole-genome comparison of disease and carriage strains provides insights
RT into virulence evolution in Neisseria meningitidis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
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; AM889137; CBA06850.1; -; Genomic_DNA.
DR AlphaFoldDB; C6SDA0; -.
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 InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
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;
FT DOMAIN 32..210
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 455 AA; 50349 MW; 298E830AB7E23273 CRC64;
MPDLHTEFSR LLPADEIAEL SPTLLKDQRN RFTSAPDIIL QPRSVESVQT IMRFCYEHRI
PVTPQGGNTG LCGAAVSENG VLLNLSKLNR IRSINLSDNC ITVEAGSVLQ TVQQAAEASN
RLFPLSLASE GSCQIGGNIA CNAGGLNVLR YGTMRDLVIG LEVVLPNGEL VSHLHPLHKN
TTGYDLRHLF IGSEGTLGII TAATLKLFAR PSDKATAWVG IPDIESAVRL LTETQAHFAE
RLCSFELIGR FAAELSSEFS KLPLPTHSEW HILLELTDSL PDSNLDDRLV EFLYKKGFTD
SVLAQSEQER IHMWALRENI SASQRKLGTS IKHDIAIPIG RVADFVRRCA KDLEQNFKGI
QIVCFGHLGD GSLHYNTFLP EILSNEVYRY ENDINDAVYR NVLACNGTIA AEHGIGIIKK
QWLDKVRTPA EIALMKSIKQ HLDPYNIMNP GKLLP
//
