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Database: UniProt
Entry: Q4PKZ9_9BACT
LinkDB: Q4PKZ9_9BACT
Original site: Q4PKZ9_9BACT 
ID   Q4PKZ9_9BACT            Unreviewed;       300 AA.
AC   Q4PKZ9;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=GlcD {ECO:0000313|EMBL:AAY81794.1, ECO:0000313|EMBL:ABI29263.1};
DE   Flags: Fragment;
GN   Name=glcD {ECO:0000313|EMBL:AAY81794.1};
OS   uncultured marine bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=56765 {ECO:0000313|EMBL:AAY81794.1};
RN   [1] {ECO:0000313|EMBL:AAY81794.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16958750; DOI=10.1111/j.1462-2920.2006.01092.x;
RA   Lau W.W., Armbrust E.V.;
RT   "Detection of glycolate oxidase gene glcD diversity among cultured and
RT   environmental marine bacteria.";
RL   Environ. Microbiol. 8:1688-1702(2006).
RN   [2] {ECO:0000313|EMBL:ABI29263.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17293517; DOI=10.1128/AEM.01965-06;
RA   Lau W.W., Keil R.G., Armbrust E.V.;
RT   "Succession and diel transcriptional response of the glycolate-utilizing
RT   component of the bacterial community during a spring phytoplankton bloom.";
RL   Appl. Environ. Microbiol. 73:2440-2450(2007).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; DQ070953; AAY81793.1; -; Genomic_DNA.
DR   EMBL; DQ070954; AAY81794.1; -; Genomic_DNA.
DR   EMBL; DQ871622; ABI29263.1; -; Genomic_DNA.
DR   EMBL; DQ871631; ABI29272.1; -; Genomic_DNA.
DR   EMBL; DQ871635; ABI29276.1; -; Genomic_DNA.
DR   EMBL; DQ871667; ABI29308.1; -; Genomic_DNA.
DR   EMBL; DQ871680; ABI29321.1; -; Genomic_DNA.
DR   EMBL; DQ871713; ABI29354.1; -; Genomic_DNA.
DR   EMBL; DQ871725; ABI29366.1; -; Genomic_DNA.
DR   EMBL; DQ871738; ABI29379.1; -; Genomic_DNA.
DR   EMBL; DQ871743; ABI29384.1; -; Genomic_DNA.
DR   EMBL; DQ871758; ABI29399.1; -; Genomic_DNA.
DR   EMBL; DQ871775; ABI29416.1; -; Genomic_DNA.
DR   EMBL; DQ871776; ABI29417.1; -; Genomic_DNA.
DR   EMBL; DQ871783; ABI29424.1; -; Genomic_DNA.
DR   EMBL; DQ871807; ABI29448.1; -; Genomic_DNA.
DR   EMBL; DQ871808; ABI29449.1; -; Genomic_DNA.
DR   EMBL; DQ871818; ABI29459.1; -; Genomic_DNA.
DR   EMBL; DQ871824; ABI29465.1; -; Genomic_DNA.
DR   EMBL; DQ871825; ABI29466.1; -; Genomic_DNA.
DR   EMBL; DQ871831; ABI29472.1; -; Genomic_DNA.
DR   EMBL; DQ871839; ABI29480.1; -; Genomic_DNA.
DR   EMBL; DQ871857; ABI29498.1; -; Genomic_DNA.
DR   EMBL; DQ871879; ABI29520.1; -; Genomic_DNA.
DR   EMBL; DQ871881; ABI29522.1; -; Genomic_DNA.
DR   EMBL; DQ871894; ABI29535.1; -; Genomic_DNA.
DR   EMBL; DQ871898; ABI29539.1; -; Genomic_DNA.
DR   EMBL; DQ871936; ABI29577.1; -; Genomic_DNA.
DR   EMBL; DQ871940; ABI29581.1; -; Genomic_DNA.
DR   EMBL; DQ871942; ABI29583.1; -; Genomic_DNA.
DR   EMBL; DQ871968; ABI29609.1; -; Genomic_DNA.
DR   EMBL; DQ871985; ABI29626.1; -; Genomic_DNA.
DR   EMBL; DQ871995; ABI29636.1; -; Genomic_DNA.
DR   EMBL; DQ872012; ABI29653.1; -; Genomic_DNA.
DR   EMBL; DQ872013; ABI29654.1; -; Genomic_DNA.
DR   EMBL; DQ872019; ABI29660.1; -; Genomic_DNA.
DR   EMBL; DQ872022; ABI29663.1; -; Genomic_DNA.
DR   EMBL; DQ872028; ABI29669.1; -; Genomic_DNA.
DR   EMBL; DQ872029; ABI29670.1; -; Genomic_DNA.
DR   EMBL; DQ872043; ABI29684.1; -; Genomic_DNA.
DR   EMBL; DQ872099; ABI29740.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4PKZ9; -.
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; 3.30.70.2740; -; 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   PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   PANTHER; PTHR42934:SF1; 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;
FT   DOMAIN          1..102
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAY81794.1"
FT   NON_TER         300
FT                   /evidence="ECO:0000313|EMBL:AAY81794.1"
SQ   SEQUENCE   300 AA;  31784 MW;  7C72F7888CCB9CB0 CRC64;
     TNLAISDAVR HLGLFYAPDP SSQIACTIGG NVAENSGGVH CLKYGLTVHN VKQLKLVSPE
     GELYEVGSRG FDGPGLDLLA LLHGSEGMLG IVVEVTVQLL PIPKNIAVVL AAFNSVNEAA
     GTVNAIISQG ILPAGLEMMD RLAIKAAEAF VNVGYPLDAE GLLICELDGT DAEVQHQIEK
     LRLILDKNNA IQVRVATDAA ERMQLWLGRK AAFPAVGRLA PDYYCMDGTI PRSELAAVLA
     QITKFSEQHG LDVANVFHAG DGNLHPLILY DANKAGEIER AEAFGADILN LCIEVGGTIT
//
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