ID S6AWZ3_PSERE Unreviewed; 467 AA.
AC S6AWZ3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=PCA10_33790 {ECO:0000313|EMBL:BAN49111.1};
OS Pseudomonas resinovorans NBRC 106553.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN49111.1, ECO:0000313|Proteomes:UP000015503};
RN [1] {ECO:0000313|EMBL:BAN49111.1, ECO:0000313|Proteomes:UP000015503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN49111.1,
RC ECO:0000313|Proteomes:UP000015503};
RX PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA Fujita N., Nojiri H.;
RT "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT resinovorans Strain CA10 (NBRC 106553).";
RL Genome Announc. 1:e00488-13(2013).
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; AP013068; BAN49111.1; -; Genomic_DNA.
DR RefSeq; WP_016493256.1; NC_021499.1.
DR AlphaFoldDB; S6AWZ3; -.
DR STRING; 1245471.PCA10_33790; -.
DR KEGG; pre:PCA10_33790; -.
DR PATRIC; fig|1245471.3.peg.3416; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_3_0_6; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000015503; Chromosome.
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; 3.30.70.2740; -; 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:SF111; D-LACTATE DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000015503}.
FT DOMAIN 46..224
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 467 AA; 49797 MW; 5AEDA30A4EA2AD20 CRC64;
MTQAPSPRQR QPLPQDLAGA LAALLGERFS TAAAVCEHHG RDESLYDPVA PDAVVFARSQ
DEISAILRLC HQHRVPVIPY GSGSSLEGHL LAVQGGISLD VSQMDQVLEF RPEDLSITVQ
PGITRKALNE YLRASGLFFP IDPGADASLG GMCATRASGT NAVRYGTMRE NVLGLTAVLA
DGRVLPTGSR AKKSSAGYDL ARLFIGSEGT LGVISEITLK LHPQPEAISA AVCSFASVDE
AVRTVIETIQ MGVPVARAEL VDALAIGALN RHFKLSLNEA PTLFLEFHGN ASSVAEQAET
VQGLAAGNGG SGFQWATQQE ERNRLWSARH NALFAFLQLK PGCRASSTDV CVPLSRLAEC
VAGTEQDLRQ SSIPAPIFGH VGDGNFHVCL LLDPDNPAEV EEAERLNRAI VQRALAVGGT
CTGEHGVGLH KMDFLLEEHG LVAIDTMRAI KQALDPLNLM NPGKIFR
//
