ID A0A290ZL42_9RHOO Unreviewed; 928 AA.
AC A0A290ZL42;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=CCZ27_07015 {ECO:0000313|EMBL:ATE59733.1};
OS Thauera sp. K11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=2005884 {ECO:0000313|EMBL:ATE59733.1, ECO:0000313|Proteomes:UP000217984};
RN [1] {ECO:0000313|EMBL:ATE59733.1, ECO:0000313|Proteomes:UP000217984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K11 {ECO:0000313|EMBL:ATE59733.1,
RC ECO:0000313|Proteomes:UP000217984};
RA Xi L., Qiao N.;
RT "Thauera phenolivorans sp. nov., a phenol derivative-degrading bacterium
RT isolated from activated sludge and an emended description of the genus
RT Thauera.";
RL Submitted (SEP-2017) 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}.
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DR EMBL; CP023439; ATE59733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A290ZL42; -.
DR KEGG; thk:CCZ27_07015; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000217984; Chromosome.
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; 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; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000217984}.
FT DOMAIN 34..262
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 530..560
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 585..608
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 928 AA; 98503 MW; D8ACD51BC15C3273 CRC64;
MSALIEALRR RLPAGRVITD ELRRLAYGTD GSFYRLIPEV VAVVDDEDEV RDVVGLARQF
RRPVTFRAAG TSLCGQAVTD GVLVLLGEGL ASCRIAADGA TVEVGPAIVG AEVNRRLAPL
GRKIGPDPAS INAAKIGGIA ANNSSGMCCG TAQNSYNTLA AIRVLFADGS LLDTGDEASV
AEFRDSRAAL LERLAALAAE VRADTELAAR IRSKYKIKNT TGYSLNALVD FDDPVDILAH
LMIGSEGTLG FISLVTYRTV PEYAHKASAL VFFPDMESAC RAVAGLKAGP VDAVELLDRA
SLRAVADKPG MPPLLLTLAD GATALLIETR APSAPGLGER VAAVLAELAN HPLLEPPAFT
TDPAEIDRLW HVRKGTFPAV GAVRKPGTTV IIEDVAVAVP DLAACCLDLQ RLFAKHGYHE
AIIFGHALEG NVHFVFTQDF GIESEVARYA AFMDEVCALL VEKYDGSLKA EHGTGRNMAP
FVELEWGARA YALMKEIKRL FDPEDLLNPG VVINDDARAH LRHLKPMPAA GALYAPVDRC
IECGFCEPQC PSHGLTLSPR QRIVGWRELA RREAAGEDAG ELGRDYLYMG LDTCATCGLC
ATACPVGIET GALTRAVRGE KLSTVARKLG QVAANHFGAT QALARTALKA GHVAESVVGT
QLLARLTGGA WKAGMPRPQP PGRVSARAGA GDKVVYFPTC AGRIFGADTP EAALSATVIR
VLERAGYAPV VPEGVDALCC GQSFVSKGMA EDADRKSAEL EAVLRRASED GRHPIVLDAS
ACSLRMKTFL AERLPVYDLV EFAHDALLPR LMLAKKAGPV LIHLNCSARR MGFEDKLTKL
ARACADEVTL PAQVKCCGFG GDRGFVVPEL NAHALRKLHA EVPAGCCGGY SSNQTCEIGL
TAATGLPYRS IVHLLDECST EAARLAAC
//
