ID A0A1M5YS48_9GAMM Unreviewed; 948 AA.
AC A0A1M5YS48;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=SAMN02745129_4371 {ECO:0000313|EMBL:SHI14906.1};
OS Ferrimonas marina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Ferrimonadaceae; Ferrimonas.
OX NCBI_TaxID=299255 {ECO:0000313|EMBL:SHI14906.1, ECO:0000313|Proteomes:UP000184268};
RN [1] {ECO:0000313|EMBL:SHI14906.1, ECO:0000313|Proteomes:UP000184268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16917 {ECO:0000313|EMBL:SHI14906.1,
RC ECO:0000313|Proteomes:UP000184268};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQXG01000008; SHI14906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5YS48; -.
DR STRING; 299255.SAMN02745129_4371; -.
DR Proteomes; UP000184268; 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; 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; 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:UP000184268}.
FT DOMAIN 47..276
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 540..571
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 597..628
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 948 AA; 103722 MW; C1EE28CAAABBDE85 CRC64;
MSSNIGVSEV SIDYQAVHQA LQAQLGEHAV TDDPVRRFAW STDGSYFRIV PELVVRVNQV
EEVEKTLAVA RQFQAPVTFR AAGTSLSGQA VGDGILVMLG YDGFRKLEIS EDHSKIALGA
AVIGADANAK LKPLDRKIGP DPATLASCMV GGIVNNNASG MCCGTAQNSY QTIDSAKLLF
ADGSYLDTGD ENSKAAFAQT HPKLLDTLTQ LAKETQADEA LSQRIRHKFS IKNTTGYSLN
ALVDFQQPFD IINHLVVGSE GTLAFVEEVT YRTVEEARFK ASAMAVFFNM VDAASAIPPL
KTDAVAAAEL LDWASIKAVT GKPGMPEWLS ELPEGAAILL IESRANDPDT LNDYTRQVTE
AIAHIQTERP IEFSSDPAVF GRYWAMRSGL FPIIGGERPK GTSVIIEDVA FRVEDLANAA
ADLSALFLEH GYPEGVIYGH ALDGNFHFII TPQFRRKSDV EQFDRFMQAV AELVINKYDG
SMKAEHGTGR AVAPFVEMEW GEQAYGLMKA IKALFDPEGL LNPGVLINDD AEVHIQRIKE
SAVVDDWVDR CIECGFCEKT CPTSALNMSP RHRITTLREI ARLEQAGEQA EAAKMREAAQ
YDVIDTCVAC QLCTIACPVD NNMGMLVRKL RSTQLTSTAQ RVLDFQADHY GSVNSVLSTG
FNVLSGMHKF TGSTVTGAIM SLGQKISSEV PYWDPDFPKG GTLPKPVQFN EDRPTVVYFA
ACGGRTFGAT PKDPDHRTLP EVMTTLLERA GYQVRVPDNT RSLCCGQMWE SKGDYKNADA
KRREMIDALE ILTEGGKYPV IVDALSCTKR TLQDAGVNYT MLDAVEFIHD ELLDKLPPVQ
KKGQVALHLG CTASHMGVND KLEAITRAFA EDVVRPAGIH CCGFAGEKGL YKPEINASAL
RHLKEQLPEK VDEGYYANRM CEVGLTRHSG ISYRHLAYLV EECTRPSA
//