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Database: UniProt
Entry: A0A081G2L3_9GAMM
LinkDB: A0A081G2L3_9GAMM
Original site: A0A081G2L3_9GAMM 
ID   A0A081G2L3_9GAMM        Unreviewed;       500 AA.
AC   A0A081G2L3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Glycolate dehydrogenase, subunit GlcD {ECO:0000313|EMBL:KEA65018.1};
DE            EC=1.1.99.14 {ECO:0000313|EMBL:KEA65018.1};
GN   ORFNames=ADIMK_0720 {ECO:0000313|EMBL:KEA65018.1};
OS   Marinobacterium lacunae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinobacterium.
OX   NCBI_TaxID=1232683 {ECO:0000313|EMBL:KEA65018.1, ECO:0000313|Proteomes:UP000028252};
RN   [1] {ECO:0000313|EMBL:KEA65018.1, ECO:0000313|Proteomes:UP000028252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK27 {ECO:0000313|EMBL:KEA65018.1,
RC   ECO:0000313|Proteomes:UP000028252};
RA   Singh A., Pinnaka A.K.;
RT   "Marinobacterium kochiensis sp. nov., isolated from sediment sample
RT   collected from Kochi backwaters in Kerala, India.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:KEA65018.1}.
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DR   EMBL; JMQN01000013; KEA65018.1; -; Genomic_DNA.
DR   RefSeq; WP_036183715.1; NZ_JMQN01000013.1.
DR   AlphaFoldDB; A0A081G2L3; -.
DR   STRING; 1232683.ADIMK_0720; -.
DR   PATRIC; fig|1232683.4.peg.712; -.
DR   eggNOG; COG0277; Bacteria.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000028252; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0019154; F:glycolate dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.465.10; -; 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: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;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Oxidoreductase {ECO:0000313|EMBL:KEA65018.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028252}.
FT   DOMAIN          47..225
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   500 AA;  53591 MW;  51FA1E9E99ECC877 CRC64;
     MSQAEANRGQ VDREALARRF RAFIDPAYVI SDDETLKPYE CDGLSVYCEM PMLVVLPETV
     EQAQQVLRIC HAEGIPVVAR GAGTGLCAGA MPHPEGVVLS MAKFNRILEI DPLARAARVQ
     PGVRNLAISE AAAVHGLYYG PDPSSQIACT IGGNVAENSG GVHCLKYGLT VHNLLSVELL
     TVEGERLSIG SEGLDSCGAD LLALLTGSEG LLGVVTEVRI KLLPKPEVAQ VVMAGFDSVQ
     TAGDAVGAII AEGIIPGGLE MMDSHAIVAA EAFAKAGYPV DAQALLLCEV DGTEEEVQEH
     IEAVENLFRR LGATSVRTSH SEEERARLWQ GRKSAFPAVG RISPDYYCMD GTIPRSQLAH
     VLTEMDKMSE ACGLRVANVF HAGDGNLHPL ILFDANVPGE LEKTEAFGAR ILELCVDVGG
     CITGEHGVGV EKIRQMPKQF NEQELSQFHR IKAAFDPAGT LNPGKGVPTL RQCQEYRSLD
     MNIEPNAGAQ AQHEGRCRHD
//
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