ID A0A037ZIS8_9RHOB Unreviewed; 472 AA.
AC A0A037ZIS8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KAJ56008.1};
GN ORFNames=ACMU_09605 {ECO:0000313|EMBL:KAJ56008.1};
OS Actibacterium mucosum KCTC 23349.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Actibacterium.
OX NCBI_TaxID=1454373 {ECO:0000313|EMBL:KAJ56008.1, ECO:0000313|Proteomes:UP000026249};
RN [1] {ECO:0000313|EMBL:KAJ56008.1, ECO:0000313|Proteomes:UP000026249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 23349 {ECO:0000313|EMBL:KAJ56008.1,
RC ECO:0000313|Proteomes:UP000026249};
RA Arahal D.R., Shao Z., Lai Q., Pujalte M.J.;
RT "Draft Genome Sequence of Actibacterium mucosum KCTC 23349, a Marine
RT Alphaproteobacterium with Complex Ionic Requirements Isolated from
RT Mediterranean Seawater at Malvarrosa Beach, Valencia, Spain.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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:KAJ56008.1}.
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DR EMBL; JFKE01000003; KAJ56008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A037ZIS8; -.
DR STRING; 1454373.ACMU_09605; -.
DR Proteomes; UP000026249; 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; 3.30.70.2190; -; 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:SF2; BLL6224 PROTEIN; 1.
DR PANTHER; PTHR43716; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000026249}.
FT DOMAIN 36..218
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 472 AA; 49644 MW; 4DA1CF9747896D56 CRC64;
MNAADPPFVS HLQSLLPAAC FRAPTPGYFE EPRGRFHGVP APVLAPATTE EVAALIRACN
SARVGVVPYG GGTGLVGGQI QPDGPAPVVL SLERMRAIRR PADPRENVLV VEAGMILADV
QAEAERVGRL FPLSLASEGS TRIGGNLSTN AGGLNVLRYG NARDLCLGIE AVLPDGTVFN
GLTRLRKDNT GYDLRNLLIG AEGTLGIITA AALKLFLQPA NRMTALFVVD SPAAALDLLA
LARDVAGEAI SAFELIGRTG FDFLTEHFPD LRQPFARPPQ WAVLTELGLS GGGDAQAALE
ALFEQAAEAG LVSDGVVAHS QAQSAALWAL RETIPAANKR IGSIASHDIS LPLSAIPDFI
ETCSTALAAL APFRINCFGH LGDGNLHYNL FPPQGQSRDA YDNIRKQATK IVHDHVHAMA
GSFSAEHGVG RMKTGDLETY GDPGKLFAMR AIKAALDPNG IMNPGAMLAQ GH
//