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Database: UniProt
Entry: A0A1H1MZG2_9CELL
LinkDB: A0A1H1MZG2_9CELL
Original site: A0A1H1MZG2_9CELL 
ID   A0A1H1MZG2_9CELL        Unreviewed;       958 AA.
AC   A0A1H1MZG2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:SDR92126.1};
GN   ORFNames=SAMN04489860_0388 {ECO:0000313|EMBL:SDR92126.1};
OS   Paraoerskovia marina.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Paraoerskovia.
OX   NCBI_TaxID=545619 {ECO:0000313|EMBL:SDR92126.1, ECO:0000313|Proteomes:UP000185663};
RN   [1] {ECO:0000313|EMBL:SDR92126.1, ECO:0000313|Proteomes:UP000185663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22126 {ECO:0000313|EMBL:SDR92126.1,
RC   ECO:0000313|Proteomes:UP000185663};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; LT629776; SDR92126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1MZG2; -.
DR   STRING; 545619.SAMN04489860_0388; -.
DR   eggNOG; COG0247; Bacteria.
DR   eggNOG; COG0277; Bacteria.
DR   Proteomes; UP000185663; Chromosome i.
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:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 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   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185663}.
FT   DOMAIN          26..261
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          525..556
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   958 AA;  100463 MW;  F81141E5E1B7A6D6 CRC64;
     MELIDDLRAA LGERAVSARA LDLHARARDA SHYLLIPEVT ATAEDAAAVG RALAVATAHR
     RPVTFRAGGT SLSGQASGTG ILLDTRQGFR RVEVLDDGAR VRVQPGATVR TVNAHLARFG
     RALGPDPASE AACTVGGVIA NNSSGMAAGT RFNSYRTLES LVIVLASGTV VDTAHPESLA
     RLREDEPRLV SVLESLRDRV RNDPSTVAEI RARFSMKNTM GYEVEALCDF DDPVKILEHL
     LVGSEGTLGF VAEAVFTTVP VQQFAATGLL VLDSVETAAA ALPALVATGA AALELMDATS
     LRVARRDPDA PAVIHGFEID RHAAILVEYR ADDETALSDL LVTGGAVLDA LPAVVPTVLT
     SDGSARAALW KVRKGLYATV AGARPAGTTA LLEDVVVPVE NLADACRDLA ALLEAHGYVD
     PVIFGHAKDG NLHFMVTEDT ESPAAVARLA AFTEDLVDLV LSHGGNLKAE HGTGRAMAPF
     IERQYSPGVV SVMREIKQAL DPSGVLNPGV VLTDDSRAHL RDLKPVDTVD AEVDRCVECG
     YCEPVCPSRD LTITPRQRIA VRRARTRAVA EGDHALVAEL DEQYEYDGID TCAADGMCAT
     ACPVKIDTGD LVKRLRQEGR GRLDKTVWRT TAEHWGATTR TAGALLDVAG RVPERLVTAP
     NSVARRALGA DTVPLWSSDL PTGGTTRTRA AGGEGVGGPV AGIFLPSCQG AMFAPAGSRT
     GGVQEAVAHL CTAAGAGLLV PDGLDSLCCG TPWSSKGYDE GHRVMTEKVL SAVGAARDEA
     RRLTGRDVPV VLDATSCTEG VAKVMEDALR AGDPRATDVV DAVAFVAEHV LPVLDIDDDR
     RVASITLHPT CSSVKGGLDT DLRTVASAIA REVHVPVDWG CCGFAGDRGM LHPELTASAT
     AAEAAEVARI GSAEHASCNR ACEIAMSRAT GRTYRHVLEV AADVVIGEVP SGAPHVTS
//
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