ID A0A085VRK1_PSESX Unreviewed; 936 AA.
AC A0A085VRK1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=IV01_00385 {ECO:0000313|EMBL:KFE58064.1};
OS Pseudomonas syringae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=317 {ECO:0000313|EMBL:KFE58064.1, ECO:0000313|Proteomes:UP000028631};
RN [1] {ECO:0000313|EMBL:KFE58064.1, ECO:0000313|Proteomes:UP000028631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAW0119 {ECO:0000313|EMBL:KFE58064.1,
RC ECO:0000313|Proteomes:UP000028631};
RA Baltrus D.A., Berge O., Morris C.;
RT "Draft Genome Sequences of Environmental Pseudomonas syringae strains.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFE58064.1}.
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DR EMBL; JPQU01000011; KFE58064.1; -; Genomic_DNA.
DR RefSeq; WP_032624936.1; NZ_JPQU01000011.1.
DR AlphaFoldDB; A0A085VRK1; -.
DR PATRIC; fig|317.175.peg.88; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000028631; 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; 102487 MW; 5D345BB8CE0F7A40 CRC64;
MSLPAAFLRD ARQLIPEQRR FDDALSTLAF GTDASFYRLI PKLVIRVESE NEVVQLLKLA
QRDKVSVTFR AAGTSLSGQA ISDSVLLVLG DNWNGRELRD EGAQIRLQPG VIGAHANAWL
APYGRKIGPD PASINACKIG GIVANNASGM CCGTAQNTYH TLAGMRLILA DGTAVDTEDP
QSVAAFRISH ADLLQQLSVL GQKTRANAEL AARIRHKYRL KNTTGLSLNA LVDYEEPLDI
LSHLLVGSEG TLGFISSVTY DTVVDHPSKA SALIVFPDVE TCCNAVTVLK TQPVAAVELL
DRRSMRSVQD KPGMPAFVRE LSSNACALLI EARAASRVLL HEQLAQIMGS LASFPVEKQV
DFTEDPVENA RLWAIRKDTF PAVGAVRLTG TTVIIEDVTF PVEQLAVGVR RLIELFDKHH
YDEAILFGHA LEGNLHFVFT QGFNNPEEVA RYQAFMEDVA QLVAVEFGGS LKAEHGTGRN
MAPFVELEWG SDAYQLMWQL KRLLDPNGIL NPDVVLSEDP QIHLKHLKPL PAADEIIDKC
IECGFCEPVC PSKGLTLSPR QRIVIWRDIQ ARKRAGINTD ELEKAYHYQG IETCAATGLC
AQRCPVGINT GELVKKLRSQ EASHRQVAGW MAQHFRTMLQ GARFTLHAAN GARMLLGAPR
LAKISAALSK ASAGRVPQWT PAMPQAEHAI SFTPPVEDQR PRVVYLAACV SRVMGPAAAD
KEQMSLMDKT RGLLEKAGYQ VVFPEDQDSL CCGQPFASKG YNEQADSKRE ELLAALSKAS
RGGLDPIYCD TSPCTLRLVQ DLKDTRLDLY DPVRFIRTHL LDKLTFTPQR EPIAVHVTCS
TQHLGESQAL IELARLCSIN VVIPEGIHCC GFAGDKGFTT PELNAHSLRS LKDAVQYCSE
GISTSRTCEI GLTQHGGIDY HGLVYLVDRV TQAKTT
//
