ID U7PA53_9GAMM Unreviewed; 950 AA.
AC U7PA53;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=Q671_04050 {ECO:0000313|EMBL:ERS91624.1};
OS Halomonas sp. PBN3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1397528 {ECO:0000313|EMBL:ERS91624.1, ECO:0000313|Proteomes:UP000017115};
RN [1] {ECO:0000313|EMBL:ERS91624.1, ECO:0000313|Proteomes:UP000017115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBN3 {ECO:0000313|EMBL:ERS91624.1,
RC ECO:0000313|Proteomes:UP000017115};
RX PubMed=24356826;
RA Overholt W.A., Green S.J., Marks K.P., Venkatraman R., Prakash O.,
RA Kostka J.E.;
RT "Draft genome sequences for oil-degrading bacterial strains from beach
RT sands impacted by the deepwater horizon oil spill.";
RL Genome Announc. 1:e01015-13(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 -!- 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:ERS91624.1}.
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DR EMBL; AXCA01000035; ERS91624.1; -; Genomic_DNA.
DR RefSeq; WP_023004751.1; NZ_AXCA01000035.1.
DR AlphaFoldDB; U7PA53; -.
DR PATRIC; fig|1397528.3.peg.589; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR eggNOG; COG0479; Bacteria.
DR Proteomes; UP000017115; 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; 3.30.70.2740; -; 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; 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 42..270
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 534..565
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 950 AA; 102588 MW; 021AC1338988A479 CRC64;
MSRPGAEAYH ELKAALSASL PGERLIDDPL RTLAYGTDAS FYRLVPRLVV RPESEAELRL
TLAECRARGL PVTFRAAGTS LSGQAVTDSV LIQLGRGWRG HEIFDEGRAI RLQPGVIGAR
ANQLLAPYGR KIGPDPASIA SCMVGGIAAN NASGMCCGTA QNSYRTVRDL RVILADGTLL
DTADPESVAA FRRSHTELLA GLERLAAETR GNAELAERIR HKYRLKNTTG YALNSLVDFS
DGIEILKHLM IGSEGTLGCI AAITYDTVVD EPLKAAALAF FPDMAATCRA TIALKRSPVS
AVELMDRAAL RSVEDEAGMP EVLRTLPEGA AALLIDVRGN DEAELQARLG EVQATLEGIR
PLEPVGFTRD ADTYALYWKI RKGLFPAVGA VRETGTTVII EDVAFPIERL DEGVLALTDI
FHRHGYAEAI LFGHALEGNL HFVFPQGFER PGEVERYQAL MDEVAQLVGV EYGGSLKAEH
GTGRNMAPYV ELEWGPEAYA LMWEIKALFD PENLLNPEVI LSRNPTLHLE NLKPLPAAHE
IVDKCIECGF CESVCPSRDL TLTPRQRIVI TRELARLEAQ GAAASDDDVA RLAALRADLG
HAVDATCAVD GLCETRCPVG INTGDLVRDM RRRRLGHHAG LARRLGAHFD GVTRAARGTL
RLAGAANRLL GDGVMGAISQ GVRRLSGERL PQWTPALPQA APVRVLKRHV DVEASRPRVV
YLPSCATRMF GADRRDDGES RSVMEVTLAL LERAGFAVVI PARVDSLCCG MAFRSKGQFD
EADHKGRELN RELLAASENG RHPILCDTSP CTLQMQEHLD DCLVLQEPVA FAHDHLLPRL
DVTPVGERVA VHVTCSSTRM GLGDKMVALA RACAEEVVVP AEITCCGFAG DKGFGVPELN
ASALSGLAEQ VAGCSAGYSN SRTCEIGLSR HGEIPYRSIL SLLDRASQPG
//
