ID H0JXL6_9NOCA Unreviewed; 463 AA.
AC H0JXL6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=D-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:EHK80911.1};
GN ORFNames=AK37_22486 {ECO:0000313|EMBL:EHK80911.1};
OS Rhodococcus pyridinivorans AK37.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1114960 {ECO:0000313|EMBL:EHK80911.1, ECO:0000313|Proteomes:UP000005064};
RN [1] {ECO:0000313|EMBL:EHK80911.1, ECO:0000313|Proteomes:UP000005064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK37 {ECO:0000313|EMBL:EHK80911.1,
RC ECO:0000313|Proteomes:UP000005064};
RA Kriszt B., Tancsics A., Cserhati M., Toth A., Nagy I., Horvath B.,
RA Tamura T., Kukolya J., Szoboszlay S.;
RL Submitted (DEC-2011) 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:EHK80911.1}.
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DR EMBL; AHBW01000061; EHK80911.1; -; Genomic_DNA.
DR RefSeq; WP_003936846.1; NZ_AHBW01000061.1.
DR AlphaFoldDB; H0JXL6; -.
DR PATRIC; fig|1114960.4.peg.4581; -.
DR Proteomes; UP000005064; Unassembled WGS sequence.
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 46..225
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 463 AA; 47597 MW; CAE65683598F3F96 CRC64;
MNPGAVTSVP DTEPAVAALV DILGDAVVTD PDRMLAYRRD QSLLTPAGMP LALVRARDTD
DVVATLTVAH RHGIPVVTRG AGTGLAGAAN ALDGGIVLSV EKMNAILEID PESRTATVQP
GVINGDLAAA AAEQGLWYVP DPGSRAVSTI GGNLATNAGG TCCAKYGVTA DHVARIKAVL
ADGQIIHTGA TTRKNVAGLN LTQLLVGSEG TLAVIVEATV RLRAAATAAA TVVASFPDTA
QAVAAVLAIR EQAEPCLVEL MDRTTIAAVE DMTHMGLDQT AGALLLVQCD GRDAAAEAEV
CALACTAAGA TEVYDTADPV EGEEFMAARR VALTALERCG STLLDDLAVP VPRLPEMLAA
VETIAARHDL LIGTFGHAAD GNLHPTIVFD AADESVARRA RQAFDEMVAE CLALGGSISG
EHGIGVLKQP YLETQVGTVE RALMHRIKAA FDPTGILNPG RGI
//
