ID H8IUR9_MYCIA Unreviewed; 461 AA.
AC H8IUR9;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Putative dehydrogenase {ECO:0000313|EMBL:AFC43376.1};
GN OrderedLocusNames=OCU_21570 {ECO:0000313|EMBL:AFC43376.1};
OS Mycobacterium intracellulare (strain ATCC 13950 / DSM 43223 / JCM 6384 /
OS NCTC 13025 / 3600).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=487521 {ECO:0000313|EMBL:AFC43376.1, ECO:0000313|Proteomes:UP000008004};
RN [1] {ECO:0000313|EMBL:AFC43376.1, ECO:0000313|Proteomes:UP000008004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600
RC {ECO:0000313|Proteomes:UP000008004};
RX PubMed=22535933; DOI=10.1128/JB.00295-12;
RA Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Lee J.H., Chun J., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare strain ATCC
RT 13950T.";
RL J. Bacteriol. 194:2750-2750(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP003322; AFC43376.1; -; Genomic_DNA.
DR RefSeq; WP_009952242.1; NZ_CP076382.1.
DR AlphaFoldDB; H8IUR9; -.
DR KEGG; mia:OCU_21570; -.
DR PATRIC; fig|487521.10.peg.2166; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_11; -.
DR Proteomes; UP000008004; Chromosome.
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 InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF2; 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 35..214
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 461 AA; 48176 MW; C8CBCE9814A773D4 CRC64;
MTDMTTRFAT IVGAHHILTG DAISDDYAHD EVLTKRPQRP AYLAKPATAD EVAQLLKAAT
ENHVPVTARG SGTGLSGAAI PRADGLLISF ERMNAVLEVD VTNQVAVVQP GVTLTALDAA
TAGTGLRYMV HPGELSSSVG GNVGTNAGGM RAVKYGIARH NVLGLQAALP TGEIIRTGGK
IAKVSTGYDL TQLIVGSEGT LALATEVIVK LHPRLDHSAT VLAPFADFDQ VMQAVPKILA
SGLAPYILEY IDNVTMAALV HTQNLELGVP DDVRDSCQAY LVVALENRTV DRLDEDVETT
GELLAELGAV DAYVLDGGAA RKLIEAREKA FWTLKALNAD DLIDAVVPRG AMPKFLSAAR
ELATGAGGAA AGCGHAGDGN VHLAIFCPDP ATRKKLLTDI FALAMELGGA ISGEHGLGRA
KAPYFVELED PVKVDLMRRI KAGFDPAGIL NPDVVFASGD A
//
