ID J3BW86_9PSED Unreviewed; 939 AA.
AC J3BW86;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=PMI33_00421 {ECO:0000313|EMBL:EJM93588.1};
OS Pseudomonas sp. GM67.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144335 {ECO:0000313|EMBL:EJM93588.1, ECO:0000313|Proteomes:UP000007281};
RN [1] {ECO:0000313|EMBL:EJM93588.1, ECO:0000313|Proteomes:UP000007281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM67 {ECO:0000313|EMBL:EJM93588.1,
RC ECO:0000313|Proteomes:UP000007281};
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:EJM93588.1}.
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DR EMBL; AKJH01000010; EJM93588.1; -; Genomic_DNA.
DR RefSeq; WP_008036544.1; NZ_AKJH01000010.1.
DR AlphaFoldDB; J3BW86; -.
DR PATRIC; fig|1144335.3.peg.398; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000007281; 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; IPR004017; Cys_rich_dom.
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; PF02754; CCG; 2.
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 939 AA; 102578 MW; 29371957FC7C5255 CRC64;
MTLPATFLRD AQQLIPQERR FDDPLSTLAF GTDASFYRLI PQLVIRVESE DEVVALLKLA
QRDQVPVTFR AAGTSLSGQA ISDSVLIVLG DNWNGREIRG HGTQIRLQPG VIGAQANAWL
APFGRKIGPD PASINACKIG GIVANNASGM CCGTAQNTYH TLAGIRLVLA DGSRLDTEDA
ASVAAFRESH AALLERLATL GRETRANSEL AAKIRHKYRL KNTTGLSLNA LVDYDEPVDI
LSHLLVGSEG TLGFISAVTY DTVIDHPNKA SALIVFPDVE TCCNAVTVLK SQPVSAVELL
DRRSLRSVQN KPGMPDFVQH LSNNACALLI ESRAASSTLL HEQLAQIMAS LTSFPVEKQV
DFTEDPIENA RLWAIRKDTF PAVGAVRKTG TTVIIEDVTF PVEQLAIGVN RLIELFDKHH
YDEAILFGHA LEGNLHFVFT QGFNNPEEVA RYQAFMDDVA QLVAVEFGGS LKAEHGTGRN
MAPFVELEWG SDAYQLMWQL KRLLDPNGIL NPDVVLSDDP QIHLKHLKPL PAADEIVDKC
IECGFCEPVC PSKGLTLSPR QRIVIWRDIQ AKKRAGVDTT ELEAAYEYQG IDTCAATGLC
AQRCPVGINT GELVKKLRGR KATHTKAASW LEGNFATALQ GARFTLHVAN GARMLLGAPR
LAKLSATLTK LSKGRVPQWT NAMPQPEKAI RFSPIVSDER PRVVYLAACV SRVMGPAAGD
KEQMSLYDKT RGLLEKAGYQ VVFPDNQDSL CCGQPFASKG YAEQAEHKRQ ELIGALLHAS
RGGLDPIYCD TSPCTLRLVQ DLGDVRLDLY DPVRFIRTHL MDRLDFTPQE APIAVHVTCS
TQHLGESQAL IDLARKCSKN VVIPEGIHCC GFAGDKGFTT PELNAHSLRT LKDAVQQCSE
GISTSRTCEI GLTQHGGIDY HGLVYLVDRV TQPRGSEEK
//
