ID R9B6Q0_9GAMM Unreviewed; 469 AA.
AC R9B6Q0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:EOR10128.1};
GN ORFNames=F896_00248 {ECO:0000313|EMBL:EOR10128.1};
OS Acinetobacter genomosp. 15BJ.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=106651 {ECO:0000313|EMBL:EOR10128.1, ECO:0000313|Proteomes:UP000016203};
RN [1] {ECO:0000313|EMBL:EOR10128.1, ECO:0000313|Proteomes:UP000016203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110321 {ECO:0000313|EMBL:EOR10128.1,
RC ECO:0000313|Proteomes:UP000016203};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. CIP 110321.";
RL Submitted (MAR-2013) 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:EOR10128.1}.
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DR EMBL; AQFL01000004; EOR10128.1; -; Genomic_DNA.
DR RefSeq; WP_016162261.1; NZ_KE007345.1.
DR AlphaFoldDB; R9B6Q0; -.
DR PATRIC; fig|1217699.3.peg.241; -.
DR HOGENOM; CLU_017779_4_1_6; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000016203; 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 42..221
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 469 AA; 52047 MW; 18DA5246ABDF32D4 CRC64;
MNASVALTPE LLTQLTAIVG ENRIKTDADS LENWGRDHTK HFDPNPSVIV FPSSTEQVQA
IVKLANQFNV AITPSGGRTG LSAGAVATNG EIVISFDKMN QILEFFPADR MVRVQAGVVT
EQLQNYAEEQ GMYYPVDFAS AGSSQIGGNI GTNAGGIKVI KYGMTRNWVL GLTVVTGKGD
VLRLNKGMIK NATGYSLQHL FIGGEGTLGL VTEAEIKLER QPQNLQVMVL GAPDFEAVMP
VLHAFQNAID LTAFEFFGEL AMQKVLDRGH VQRPFETQCP FYVLLEFEAP YEPIMDKAMQ
IFEHCMEQGW VIDGVMSQSL EQAQSLWRLR EDISESIAPF IPYKNDISVL ITHVPAFIAE
IDAIVADNYP DFEICWFGHI GDGNLHLNIL KPENLTKDEF FAKCQVVNKY VFETVKKYDG
SISAEHGVGM TKKPYLEYSR SPEEIEYMKA LKLAFDPNGI MNPGKLFDL
//
