ID V9VV41_9RHOB Unreviewed; 472 AA.
AC V9VV41;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=D-2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:AHD01594.1};
GN ORFNames=METH_13645 {ECO:0000313|EMBL:AHD01594.1};
OS Leisingera methylohalidivorans DSM 14336.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD01594.1, ECO:0000313|Proteomes:UP000018780};
RN [1] {ECO:0000313|EMBL:AHD01594.1, ECO:0000313|Proteomes:UP000018780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD01594.1,
RC ECO:0000313|Proteomes:UP000018780};
RG DOE Joint Genome Institute;
RA Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; CP006773; AHD01594.1; -; Genomic_DNA.
DR RefSeq; WP_024090946.1; NC_023135.1.
DR AlphaFoldDB; V9VV41; -.
DR STRING; 999552.METH_13645; -.
DR KEGG; lmd:METH_13645; -.
DR PATRIC; fig|999552.6.peg.2727; -.
DR HOGENOM; CLU_017779_4_1_5; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000018780; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; 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; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 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 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT DOMAIN 38..219
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 49621 MW; FC64AE734C190FA6 CRC64;
MSLNPADTAF ATRLSNQLPE GVLRPPEPRY LEEPRGRYRG QAGVLALPQT VEHVSVLIRE
ANAARVPVVP YGGGTGLVGG QVMPDGPAPL VLSLERMTAI RSVFPQENVL IAEAGAILAD
IQTAAQGAGR LFPLSLAAEG SARIGGNLST NAGGVNVLRY GNARDLCLGL EAVLPTGEIW
QGLSRLRKDN TGYDLKNLLI GAEGTLGVIT AAALKLSPIP VSQGTAFFTV KDPAAAIALL
ALARDHAGEA VSAFELIHRQ GLDFLSDCLP QIRQPFAEAP EWSVLIELGL PRGLDPEETL
AELFEAAAAA GLAGDGVIAQ SGSQRQALWA VRENIPAANK AIGSVSSHDI SVPVSDIPAF
IERGSEVVAG LGDFRINCFG HLGDGNLHYN VFPSKGHMRE EYNHLRGAVK EAVHDLVHAF
GGSFSAEHGV GRMKTGDLER YGDPVRLAAM RAIKLALDPN GIMNPGAVLK TG
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