GenomeNet

Database: UniProt
Entry: M7MTF7_9MICC
LinkDB: M7MTF7_9MICC
Original site: M7MTF7_9MICC 
ID   M7MTF7_9MICC            Unreviewed;       558 AA.
AC   M7MTF7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Glycolate oxidase subunit {ECO:0000313|EMBL:EMQ98220.1};
DE            EC=1.1.3.15 {ECO:0000313|EMBL:EMQ98220.1};
GN   ORFNames=ADIAG_02236 {ECO:0000313|EMBL:EMQ98220.1};
OS   Paeniglutamicibacter gangotriensis Lz1y.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Paeniglutamicibacter.
OX   NCBI_TaxID=1276920 {ECO:0000313|EMBL:EMQ98220.1, ECO:0000313|Proteomes:UP000012015};
RN   [1] {ECO:0000313|EMBL:EMQ98220.1, ECO:0000313|Proteomes:UP000012015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lz1y {ECO:0000313|EMBL:EMQ98220.1,
RC   ECO:0000313|Proteomes:UP000012015};
RX   PubMed=23766407;
RA   Shivaji S., Ara S., Bandi S., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Arthrobacter gangotriensis Strain Lz1yT, Isolated
RT   from a Penguin Rookery Soil Sample Collected in Antarctica, near the Indian
RT   Station Dakshin Gangotri.";
RL   Genome Announc. 1:e00347-e00313(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
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:EMQ98220.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AOCK01000006; EMQ98220.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7MTF7; -.
DR   STRING; 1276920.ADIAG_02236; -.
DR   PATRIC; fig|1276920.7.peg.2239; -.
DR   eggNOG; COG0277; Bacteria.
DR   Proteomes; UP000012015; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProt.
DR   GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.300.330; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.3450; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR025650; Alkyl-DHAP_Synthase.
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; PTHR46568; ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL; 1.
DR   PANTHER; PTHR46568:SF1; ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL; 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|PIRSR:PIRSR625650-3};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR625650-3};
KW   Oxidoreductase {ECO:0000313|EMBL:EMQ98220.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012015}.
FT   DOMAIN          106..288
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        472
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT   BINDING         272..278
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         411
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT   SITE            326
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ   SEQUENCE   558 AA;  58508 MW;  14DDF30DD764D7B2 CRC64;
     MVTQNTVEIP RSVWYGWGDP AHATSLSANA LTYLSATLKL ASVKPVHPPA DITEVRIGEP
     VLNAEALAEL RAACGTEYVS TERLDRIEHS GGKSTEDLLR IRAGDALGAP DAVIFPASSE
     EIREVLAVCA ARGIAVTAFG GGTSVVGGVS PLRGTFDAAI TLDMRRMNKM LHLDPRSRTA
     TFEAGLRGPG IEAALEPHGF TLGHFPQSHQ EATLGGYVAT RSAGQASTGY GRSDDLVKSV
     HLETPAGPLV AGSTAPGTAA GPKLLDVIVG SEGAFGVITS ATLKIVPVPT HKSYGSWSFA
     SFTAGAEAIR RLRHEGLSGD LPHVCRLSDS DETASTFKLG GPKTAALGKY LSVRGQATPA
     LALFLWEGAT KETAARKRRS ARILRAAGGI PTGPIPARAW EHGRFSGPYL RDELLTRGVY
     VETLETSATW TSLDSTYHAV REAILKSLAE HGGTGYVQSH ISHIYPDGAS LYFTYLAGVE
     SDGLAQHARV KQAASKAIVA AGSTITHHHS VGTDHAPYLG AEIGALGLDV LRGIKNTLDP
     AGIMNPGKLI PAAIKEQP
//
DBGET integrated database retrieval system