ID I1CWS6_9PSEU Unreviewed; 396 AA.
AC I1CWS6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative dehydrogenase {ECO:0000313|EMBL:EIE97150.1};
GN ORFNames=SacglDRAFT_00187 {ECO:0000313|EMBL:EIE97150.1};
OS Saccharomonospora glauca K62.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=928724 {ECO:0000313|EMBL:EIE97150.1, ECO:0000313|Proteomes:UP000005087};
RN [1] {ECO:0000313|EMBL:EIE97150.1, ECO:0000313|Proteomes:UP000005087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K62 {ECO:0000313|EMBL:EIE97150.1,
RC ECO:0000313|Proteomes:UP000005087};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Brambilla E., Klenk H.-P., Woyke T.J.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K62 {ECO:0000313|Proteomes:UP000005087};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA Klenk H.-P., Woyke T.;
RT "Noncontiguous Finished sequence of chromosome of Saccharomonospora glauca
RT K62.";
RL Submitted (JAN-2012) 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 L2HGDH family.
CC {ECO:0000256|ARBA:ARBA00037941}.
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DR EMBL; CM001484; EIE97150.1; -; Genomic_DNA.
DR RefSeq; WP_005460925.1; NZ_CM001484.1.
DR AlphaFoldDB; I1CWS6; -.
DR STRING; 928724.SacglDRAFT_00187; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_024775_0_1_11; -.
DR OrthoDB; 9801699at2; -.
DR Proteomes; UP000005087; Chromosome.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43104:SF2; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005087}.
FT DOMAIN 4..391
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 396 AA; 42688 MW; 081C4991EB6CDF40 CRC64;
MRHVTVIGGG IIGLAVAWKL TGRGYRVTVL EKEDHWAAHQ TGHNSNVVHA GLYYRPGSLK
ARLSVAGNRS MVAFAREHGV PVEVCGKLVV ATSEAELPAL GVLAERAEAN GVPATMLEPA
QAAEYEPEVT CVRALRVHST AVIDFPAVCR VLATLARDAG ADLRLNSPAL GIRTGDRGGV
EVATPHGVVA SDVLVNCAGL HSDRVARLAG FTPSARIVPF RGEYYTLRPE RRHLVRGLIY
PVPDPALPFL GVHLTRMLDG SVHAGPNAVP ALRREGYRWR DVSPGDLLDT LTFPGTWRFA
RRYAFPVGWD EVRRSLSKRR FAASLARLVP AVTPDDIVRH DSGVRAQALL PDGRLADDFL
VEESRGQVHV LNAPSPAATS ALEIASHIVD RVTAHA
//
