ID Q5F817_NEIG1 Unreviewed; 455 AA.
AC Q5F817;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AAW89670.1};
GN ORFNames=NGO_0984 {ECO:0000313|EMBL:AAW89670.1};
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89670.1, ECO:0000313|Proteomes:UP000000535};
RN [1] {ECO:0000313|Proteomes:UP000000535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535};
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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; AE004969; AAW89670.1; -; Genomic_DNA.
DR RefSeq; WP_003702575.1; NC_002946.2.
DR RefSeq; YP_208082.1; NC_002946.2.
DR AlphaFoldDB; Q5F817; -.
DR STRING; 242231.NGO_0984; -.
DR KEGG; ngo:NGO_0984; -.
DR PATRIC; fig|242231.10.peg.1153; -.
DR HOGENOM; CLU_017779_4_1_4; -.
DR Proteomes; UP000000535; 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 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000000535}.
FT DOMAIN 32..210
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 455 AA; 50270 MW; B848755699B2B471 CRC64;
MPDLHTEFSR LLPADEIAEP SPTLLKDQRN RFTSAPDIIL QPRSVESVQT IMRFCYEHRI
PVTPQGGNTG LCGAAVSENG VLLNLSKLNR IRSINLSDNC ITVEAGSVLQ TVQQAAEASN
RLFPLSLASE GSCQIGGNIA CNAGGLNVLR YGTMRDLVIG LEVVLPNGEL VSHLHPLHKN
TTGYDLRHLF IGSEGTLGII TAATLKLFAR PSDKATAWVG IPDIESAVRL LTETQAHFAE
RLCSFELIGR FAAKLSSEFS KLPLPTHSEW HILLELTDSL PDSNLDDRLV EFLYKKGFTD
SVLAQSEQER IHMWALRENI SASQRKLGTS IKHDIAVPIG RVADFVRQCA KDLEQNFKGI
QIVCFGHLGD GSLHYNTFPP EILSNEVYRY ENDINSTVYR NVLARNGTIA AEHGIGIIKK
QWLPAVRTPS EIALMKSIKQ HLDPYNIMNP GKLLP
//
