ID E6THT4_MYCSR Unreviewed; 502 AA.
AC E6THT4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Glycine/D-amino acid oxidase, deaminating {ECO:0000313|EMBL:ADT96833.1};
GN OrderedLocusNames=Mspyr1_01000 {ECO:0000313|EMBL:ADT96833.1};
OS Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
OS (Mycobacterium gilvum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=278137 {ECO:0000313|EMBL:ADT96833.1, ECO:0000313|Proteomes:UP000008916};
RN [1] {ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L.,
RA Koukkou A.I., Drainas C., Kyrpides N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium sp. Spyr1.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADT96833.1, ECO:0000313|Proteomes:UP000008916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC {ECO:0000313|Proteomes:UP000008916};
RX PubMed=22180818;
RA Kallimanis A., Karabika E., Mavromatis K., Lapidus A., Labutti K.M.,
RA Liolios K., Ivanova N., Goodwin L., Woyke T., Velentzas A.D.,
RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT "Complete genome sequence of Mycobacterium sp. strain (Spyr1) and
RT reclassification to Mycobacterium gilvum Spyr1.";
RL Stand. Genomic Sci. 5:144-153(2011).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
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DR EMBL; CP002385; ADT96833.1; -; Genomic_DNA.
DR RefSeq; WP_013470328.1; NC_014814.1.
DR AlphaFoldDB; E6THT4; -.
DR KEGG; msp:Mspyr1_01000; -.
DR HOGENOM; CLU_007884_15_0_11; -.
DR Proteomes; UP000008916; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR PANTHER; PTHR13847:SF274; RIESKE 2FE-2S IRON-SULFUR PROTEIN YHFW-RELATED; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 451..502
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 502 AA; 53718 MW; 55712CBA5D6739C4 CRC64;
MSSLWTDGRV ETPSRPDEVA AVRTADVVVV GAGITGLTTA LLLAHAGKKV VVVEARHIGA
CATGNTTGKV SVLQGSKLAN VAGKHGTDTL RAYVLGNTEG RDWLLRYCDE HGISAQREDD
HAYAQNEKGL GTARKILAAC REANLDAQWV DEADVPFPFA GGVRLREQAQ IDPMPYLSSV
VTELERHGGT VLQGVRATSV SGVRSVTVTL RMTTRPDDTR DEDFSITAER CVLATGIPVL
DRGFFFARAE PMRSYCMAFD VPGELTRSMY ISVDSPTRSV RYAPVPGGEK LIVGGAGHPV
GRADDPKSAV DELARWATLH YPGAVQTHFW SAQDYHPADE LPYVGPLLPK LENILVATGF
DKWGMTNGVA AALALTSRIL GGRMDWAQAF ASWSPHELSG IPTALQMNFE VGLHLAKGWV
TPVTTPAGPP GEGEGIVTGP PWNLRACSVV DGVERTVSPV CPHLGGIVEW NNIDHAWECP
LHGSRFAPDG TLLEGPATRG LT
//
