ID J3FTW7_9PSED Unreviewed; 809 AA.
AC J3FTW7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=PMI26_02045 {ECO:0000313|EMBL:EJM44475.1};
OS Pseudomonas sp. GM33.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144329 {ECO:0000313|EMBL:EJM44475.1, ECO:0000313|Proteomes:UP000007274};
RN [1] {ECO:0000313|EMBL:EJM44475.1, ECO:0000313|Proteomes:UP000007274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM33 {ECO:0000313|EMBL:EJM44475.1,
RC ECO:0000313|Proteomes:UP000007274};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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 -!- 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:EJM44475.1}.
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DR EMBL; AKJO01000070; EJM44475.1; -; Genomic_DNA.
DR AlphaFoldDB; J3FTW7; -.
DR PATRIC; fig|1144329.3.peg.2022; -.
DR Proteomes; UP000007274; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; IPR009051; Helical_ferredxn.
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 Pfam; PF13183; Fer4_8; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}.
FT DOMAIN 37..265
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 529..560
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 809 AA; 88304 MW; 096F7243591F1F1D CRC64;
MSLPAAFLRD AQQLIPQERR FDDPLSTLAF GTDASFYRLI PQLVIRVESE DEVVALLQLA
QRDQVPVTFR AAGTSLSGQA ISDSVLIVLG DNWNAREIRD QGTQIRLQPG VIGAQANAWL
APFGRKIGPD PASINACKIG GIVANNASGM CCGTAQNTYH TLAGIRLVLA DGSRLDTEDA
ASVAAFRQSH AALLERLATL GRETRANADL AARIRHKYRL KNTTGLSLNA LVDFDEPVDI
LSHLLVGSEG TLGFISAVTY DTVIDHPNKA SALIVFPDVE TCCNAVTVLK SQPVSAVELL
DRRSLRSVQD KPGMPSFVQH LSNNACALLI ESRAASSALL HEQLAQIMAS LQTFPVEKQV
DFTEDPRENA RLWAIRKDTF PAVGAVRKTG TTVIIEDVTF PVEQLAIGVN RLIELFDKHH
YDEAILFGHA LEGNLHFVFT QGFNNTEEVA RYQAFMDDVA QLVAVEFGGS LKAEHGTGRN
MAPFVELEWG SDAYQLMWQL KRLLDPNGIL NPDVVLSDDP QIHLKHLKPL PAADEIVDKC
IECGFCEPVC PSKGLTLSPR QRIVIWRDIQ AKKRAGIDTT ELEAAYEYQG IDTCAATGLC
AQRCPVGINT GELVKKLRSR TATHTKTANW LEGNFATALQ GARFTLHVAN GARMLLGAPR
LAKLSSTLTK LSKGQVPQWT NAMPQPEKAI RFSPAVSDER PRVVYLAACV SRVMGPAAGD
KEQVSLYDKT RGLLEKAGYQ VVFPDNLDNL CCGQPFASKG YAEHAEHKRQ ELIGALLHAS
RGGLDPIYCD TSPCTLRLTQ DLGDVRLDL
//
