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Database: UniProt
Entry: K6D7H4_9BACI
LinkDB: K6D7H4_9BACI
Original site: K6D7H4_9BACI 
ID   K6D7H4_9BACI            Unreviewed;       468 AA.
AC   K6D7H4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Glycolate oxidase subunit {ECO:0000313|EMBL:EKN64259.1};
GN   ORFNames=BABA_23460 {ECO:0000313|EMBL:EKN64259.1};
OS   Neobacillus bataviensis LMG 21833.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN64259.1, ECO:0000313|Proteomes:UP000006316};
RN   [1] {ECO:0000313|EMBL:EKN64259.1, ECO:0000313|Proteomes:UP000006316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT   reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EKN64259.1}.
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DR   EMBL; AJLS01000148; EKN64259.1; -; Genomic_DNA.
DR   RefSeq; WP_007087683.1; NZ_AJLS01000148.1.
DR   AlphaFoldDB; K6D7H4; -.
DR   STRING; 1117379.BABA_23460; -.
DR   PATRIC; fig|1117379.3.peg.4868; -.
DR   eggNOG; COG0277; Bacteria.
DR   OrthoDB; 9767256at2; -.
DR   Proteomes; UP000006316; Unassembled WGS sequence.
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   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; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006316}.
FT   DOMAIN          36..215
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   468 AA;  51064 MW;  067A28DEFB08E0B0 CRC64;
     MDVKAIIQTI QSIIPEQRIL TQLADRYSYS FDASFGEYLP DLVIQPQTKE EISSILKLAN
     EHRIPIYPRG AATSLSGGPL PVEGGIVLDM SQFPKKLIID QENLLAIVSP SVITGDIHKL
     AEEGDLFYPP DPSSSHVSTI GGNLLENSSG PKGLKYGTTK EYVIGLEVVT PTGEIIRTGG
     KTVKNVTGYD LTRLIVGSEG TLGIVTEAVL RLIPKPQARK TLLASFGRLI DSGHAITNIL
     SSGILPSAME LMDHACIQAV ENYTKSGLPL DAEAIVIIEV DGHAAAIEDE IKKCAEICRK
     ENASDILVAE DDTERDKIWH ARKMVSPAIA KMGPTKISED ATVPRSQIPK MIERLHAIRE
     KYQLNLVVFG HAGDGNLHPN IITDKRNIEE MKRAEAAISE IFEAAVELGG TLSGEHGIGL
     LKAPYMEMEL GKEGLRFMKL IKEAWDPNHI LNPGKIFPKP EQTRVVLI
//
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