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}.
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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
//