ID C6M397_NEISI Unreviewed; 455 AA.
AC C6M397;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=FAD linked oxidase, C-terminal domain protein {ECO:0000313|EMBL:EET45361.1};
GN ORFNames=NEISICOT_00988 {ECO:0000313|EMBL:EET45361.1};
OS Neisseria sicca ATCC 29256.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=547045 {ECO:0000313|EMBL:EET45361.1, ECO:0000313|Proteomes:UP000005365};
RN [1] {ECO:0000313|EMBL:EET45361.1, ECO:0000313|Proteomes:UP000005365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29256 {ECO:0000313|EMBL:EET45361.1,
RC ECO:0000313|Proteomes:UP000005365};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUL-2009) 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}.
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:EET45361.1}.
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DR EMBL; ACKO02000004; EET45361.1; -; Genomic_DNA.
DR RefSeq; WP_003756943.1; NZ_ACKO02000004.1.
DR AlphaFoldDB; C6M397; -.
DR STRING; 490.A6J88_11470; -.
DR eggNOG; COG0277; Bacteria.
DR Proteomes; UP000005365; Unassembled WGS sequence.
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}.
FT DOMAIN 32..210
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 455 AA; 49857 MW; 1D269833CC888651 CRC64;
MPNLYDRFLE FLSPAEILEA TPALLNDQRR RFVSEPDIIL QPHSIENVQE IMRFCFEHRI
PVTPQGGNTG LCGAAVASGG VLLNLSKINR IREINLADNS ITVEAGVILQ NVQKAAAEAG
RLFPLSLASE GSCEIGGNIA CNAGGLNVLR YGSMRDLVLG LEVVLPNGEL VSHLQPLHKN
TTGYDLRHLF IGSEGTLGII TAATLKLFAR PQTTATAWVG LDDIESAVEL LTAVQGHFAE
RLTSFELISR YALALSSEFS RLKQPTDANW HVLLELTDSV PDAALDEKLA EFLYQNGQEN
SIIAQSEQER LDLWTLRENI SASQRKLGTS IKHDIAVPIA QVATFVRQCA PALETRFPGI
QIVCFGHLGD GSLHYNTFLP DVLSNEAYRY EDAVNTIVYE HILACHGTIA AEHGIGTIKK
HWLPSVRTPS EIALMRAIKA QLDPHDIMNP GKLLP
//
