ID J3EZF2_9PSED Unreviewed; 936 AA.
AC J3EZF2;
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=PMI21_00235 {ECO:0000313|EMBL:EJM22052.1};
OS Pseudomonas sp. GM18.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144324 {ECO:0000313|EMBL:EJM22052.1, ECO:0000313|Proteomes:UP000007280};
RN [1] {ECO:0000313|EMBL:EJM22052.1, ECO:0000313|Proteomes:UP000007280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM18 {ECO:0000313|EMBL:EJM22052.1,
RC ECO:0000313|Proteomes:UP000007280};
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:EJM22052.1}.
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DR EMBL; AKJT01000004; EJM22052.1; -; Genomic_DNA.
DR RefSeq; WP_007933484.1; NZ_AKJT01000004.1.
DR AlphaFoldDB; J3EZF2; -.
DR PATRIC; fig|1144324.3.peg.228; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000007280; 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 936 AA; 102120 MW; 3154F916239682FB CRC64;
MSLPAAFLRD AQQLIPEARR FDDPLSTLAF GTDASFYRLI PKLVIRVESE DEVVALLKLA
QRDQVPVTFR AAGTSLSGQA ISDSVLIVLG DNWNGREIRG QGTRIRLQPG VIGAQANAWL
APFGRKIGPD PASINACKIG GIVANNASGM CCGTAQNTYH TLAGIRLVLA DGSRLDTEDA
SSVAAFRESH AELLERLATL GRETRANAEL AAKIRHKYRL KNTTGLSLNA LVDFDEPVDI
LSHLLVGSEG TLGFISAVTY DTVIDHPNKA SALIVFPDVE TCCNAVTVLK SQPVSAVELL
DRRSLRSVQD KPGMPAFVQQ LSTNACALLI ESRAASSTLL QEQLAQIMAS LMGFPVEKQV
DFTEDPLENA RLWAIRKDTF PAVGAVRKTG TTVIIEDVTF PVEQLAIGVN RLIELFDKHH
YDEAILFGHA LEGNLHFVFT QGFNSAEEVA RYQAFMDDVA QLVAVEFGGS LKAEHGTGRN
MAPFVELEWG SDAYQLMWQL KRLLDPNGIL NPDVVLSDDP QIHLKHLKPL PAADEIVDKC
IECGFCEPVC PSKGLTLSPR QRIVIWRDIQ AKKRAGIDTA ELEQAYEYQG IDTCAATGLC
AQRCPVGINT GELVKKLRGR NATHTKTANW IEGNFATALQ GARFTLHVAN GARMLLGAPR
LAKLSATLTR LSKGQVPQWT NAMPQPEKAI RFSPSVSDER PRVVYLAACV SRVMGPAAGD
KEQMSLYDKT RGLLEKAGYQ VVFPDNQDNL CCGQPFASKG YAEQAEHKRQ ELIGALLHAS
RGGLDPIYCD TSPCTLRLVQ DLGDVRLDLY DPVRFIRTHL IDRLDFTPQE APIAVHVTCS
TQHLGESQAL IDLARKCSKN VVIPEGIHCC GFAGDKGFTT PELNAHSLRT LKDAVQQCSE
GISTSRTCEI GLTQHGGIDY HGLVYLVDRV TRARAV
//
