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Database: UniProt
Entry: A0A1M5YS48_9GAMM
LinkDB: A0A1M5YS48_9GAMM
Original site: A0A1M5YS48_9GAMM 
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}.
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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
//
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