ID A0A0P0NX06_9CAUL Unreviewed; 469 AA.
AC A0A0P0NX06;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:ALL12113.1};
GN ORFNames=AQ619_01360 {ECO:0000313|EMBL:ALL12113.1};
OS Caulobacter henricii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=69395 {ECO:0000313|EMBL:ALL12113.1, ECO:0000313|Proteomes:UP000056905};
RN [1] {ECO:0000313|EMBL:ALL12113.1, ECO:0000313|Proteomes:UP000056905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB4 {ECO:0000313|EMBL:ALL12113.1,
RC ECO:0000313|Proteomes:UP000056905};
RA Scott D., Ely B.;
RT "Conservation of the essential genome among Caulobacter and Brevundimonas
RT species.";
RL Submitted (OCT-2015) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013002; ALL12113.1; -; Genomic_DNA.
DR RefSeq; WP_062143186.1; NZ_CP013002.1.
DR AlphaFoldDB; A0A0P0NX06; -.
DR STRING; 69395.AQ619_01360; -.
DR KEGG; chq:AQ619_01360; -.
DR eggNOG; COG0277; Bacteria.
DR OrthoDB; 9809290at2; -.
DR Proteomes; UP000056905; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000056905}.
FT DOMAIN 40..218
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 469 AA; 49299 MW; 6F75F4613322CE69 CRC64;
MTKPVPADTL SRLKAVLGEG GWSQDPERLE PKLLEWRGRW RGETPLLVLP RTTGEVAAVV
GICAADGVAI TPQGGNTGLV AGQIPQGEIL LSTEKLRAVR DVDGLDDVMV LEAGVTLSEA
HARAASVGRR FTVGVASEGS CTIGGLVSTN AGGTAVLRYG MMREQVLGLE AVLPNGEIWN
GLKRLRKDNT GYDLKQLLIG AEGTLGVVTA ASLKLHPLLA SRAVAIVGLG SPEDAIQLLA
RAKDETGGAV EAFELMGRLG FELTLRNVPG LRDPLPSIHP WYVLIEIASG EPGAAEAALE
RLLASALERG LISDAAVAQT QTQMKAFWHI REGHSAGQKP EGAAWKHDVS VPVSKIPVFI
ARANAAIAAA YPGTRIVAFG HVGDGNVHYD VIKPAGGDDD AHDAQRDAGA SIVHDITADL
NGSISAEHGL GAMKTIEAVG YKDPVELTAL RAIRSALDPQ RIMNPRVLF
//
