ID G5ZWS9_9PROT Unreviewed; 393 AA.
AC G5ZWS9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=FAD/FMN-dependent dehydrogenase {ECO:0000313|EMBL:EHI49512.1};
GN ORFNames=HIMB100_00004730 {ECO:0000313|EMBL:EHI49512.1};
OS SAR116 cluster alpha proteobacterium HIMB100.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster.
OX NCBI_TaxID=909943 {ECO:0000313|EMBL:EHI49512.1, ECO:0000313|Proteomes:UP000004261};
RN [1] {ECO:0000313|EMBL:EHI49512.1, ECO:0000313|Proteomes:UP000004261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain HIMB100 {ECO:0000313|Proteomes:UP000004261};
RX PubMed=22675578; DOI=10.4056/sigs.1854551;
RA Grote J., Bayindirli C., Bergauer K., Carpintero de Moraes P., Chen H.,
RA D'Ambrosio L., Edwards B., Fernandez-Gomez B., Hamisi M., Logares R.,
RA Nguyen D., Rii Y.M., Saeck E., Schutte C., Widner B., Church M.J.,
RA Steward G.F., Karl D.M., Delong E.F., Eppley J.M., Schuster S.C.,
RA Kyrpides N.C., Rappe M.S.;
RT "Draft genome sequence of strain HIMB100, a cultured representative of the
RT SAR116 clade of marine Alphaproteobacteria.";
RL Stand. Genomic Sci. 5:269-278(2011).
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:EHI49512.1}.
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DR EMBL; AFXB01000004; EHI49512.1; -; Genomic_DNA.
DR AlphaFoldDB; G5ZWS9; -.
DR STRING; 909943.HIMB100_00004730; -.
DR PATRIC; fig|909943.3.peg.485; -.
DR eggNOG; COG0277; Bacteria.
DR Proteomes; UP000004261; 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 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; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000004261}.
FT DOMAIN 1..181
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 393 AA; 41814 MW; 53BEBF7F97309DBD CRC64;
MTIWQPETGE QVTEIISSAL AQQRPMRICS HDTKLGFGTP VGTDDTLSLK ALSGVIDYQP
EELVLVVKAG TPLVDIEQLL AEQNQMLAFE PPHLDGFYSS EGTGTIAGVV ATNLSGPRRV
SAGAARDFLL GFSAVSGRGD EFKSGSRVMK NVTGYDLSKL ICGSFGTLAV MTDITLKVLP
RPETSSSLSV QCESLRSAQA VLSAAFCTDT EPSGGAIART EAGWRAVIRL EGVDVSVRDR
MTSLKTALSA HGEQTTLDLP ASEAFWQSWC DLSMIPSEAE QVYKISVAPS DAPALLDHLL
KSYNLHVSLD WAGGLIWIAG QGEELCGAVR DAVAACGNGH VTLMRGSEQL RSEQAVFQPQ
AAALAALSHR IKTAFDPQHI LNPGKMGEMR GGV
//
