ID Q2YII4_BRUA2 Unreviewed; 410 AA.
AC Q2YII4;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=FAD linked oxidase, C-terminal:FAD linked oxidase, N-terminal {ECO:0000313|EMBL:CAJ12341.1};
GN Name=glcE {ECO:0000313|EMBL:CAJ12341.1};
GN OrderedLocusNames=BAB2_0175 {ECO:0000313|EMBL:CAJ12341.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ12341.1, ECO:0000313|Proteomes:UP000002719};
RN [1] {ECO:0000313|EMBL:CAJ12341.1, ECO:0000313|Proteomes:UP000002719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 {ECO:0000313|EMBL:CAJ12341.1,
RC ECO:0000313|Proteomes:UP000002719};
RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG Microbial Genomics Group;
RG Lawrence Livermore National Laboratory;
RG and the Genome Analysis Group;
RG Oak Ridge National Laboratory;
RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AM040265; CAJ12341.1; -; Genomic_DNA.
DR RefSeq; WP_002966401.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YII4; -.
DR STRING; 359391.BAB2_0175; -.
DR GeneID; 3828235; -.
DR KEGG; bmf:BAB2_0175; -.
DR PATRIC; fig|359391.11.peg.2124; -.
DR HOGENOM; CLU_017779_0_0_5; -.
DR Proteomes; UP000002719; Chromosome II.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 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 PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002719}.
FT DOMAIN 1..185
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 410 AA; 44075 MW; 8CDE660137B61764 CRC64;
MSDANILKPQ DEAGVLEMVQ AALASSTPLE IIGHGSKRGI GRPVEAGHVL DVSGLSGVTL
YEPDELVLSA RAGTPMAEIQ KLLADHNQCF HFEPMDYGPL LGAEPGRGTI GGTLAANLAG
PRRLKAGAAR DHVLGVRVVS GRGEVFKSGG RVVKNVTGYD LSKGMANSWG TLGVATEVTF
KVLPAPETVA TLAVRGLDDE QAARVMALAM GSREEVSSAA HLPPTVAWRF LDGKLGGDAA
TILRLEGFAP SVAHRSRQLQ DLLGRTGTID VLDDSQSRQL WREVRDVLPY AQAGDGRAVW
RVSMAPMQGW RMVDEFRRHA GVDAYYDWQG GLIWMRMEAE PEADVLRKLI ARHGGGHATL
IRAPERVRGS VDVFQQQPAA LAALSARLKQ QFDPENILNP GRMYPHQAGA
//
