ID   A0A0M0I492_9VIBR        Unreviewed;       945 AA.
AC   A0A0M0I492;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE            EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN   ORFNames=AKJ31_01850 {ECO:0000313|EMBL:KOO09130.1};
OS   Vibrio hepatarius.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=171383 {ECO:0000313|EMBL:KOO09130.1, ECO:0000313|Proteomes:UP000037530};
RN   [1] {ECO:0000313|Proteomes:UP000037530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19134 {ECO:0000313|Proteomes:UP000037530};
RA   Giubergia S., Machado H., Mateiu R.V., Gram L.;
RT   "Vibrio galatheae sp. nov., a novel member of the Vibrionaceae family
RT   isolated from the Solomon Islands.";
RL   Submitted (AUG-2015) 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   -!- 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:KOO09130.1}.
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DR   EMBL; LHPI01000001; KOO09130.1; -; Genomic_DNA.
DR   RefSeq; WP_053407383.1; NZ_LHPI01000001.1.
DR   AlphaFoldDB; A0A0M0I492; -.
DR   STRING; 171383.AKJ31_01850; -.
DR   PATRIC; fig|171383.3.peg.383; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000037530; 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; 3.30.70.2190; -; 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; 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; 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          43..271
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          535..566
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   945 AA;  103693 MW;  5BCC36914044838D CRC64;
     MANSITPATY EQLEELLALH IEPERIITQE AKRLAYGTDA SFYRLVPKIV LRLKNLDEVI
     YAIQSCREMG VHFTFRAAGT SLSGQAVSDS VLITLTDDWR GHEIIDNGDK IILQPGVIGA
     DANKYLAPFQ RKIGPDPASI NTCKIGGIAA NNASGMCCGT AQNSYRTIDS IKVVFSDGTL
     LDTASKESID AFKVTRPDII EGLQSLVAET QRNQELSERI RHKYRLKNTT GYALNALVDF
     NDPIEVLEHL LIGSEGTLGF IAEITYNTVI EHAHKASSLL VFADIEEASE AVTTLSKTPV
     AAVELMDGRA LRSVADKPGM PAFIPELDLE AAALLVESHA SSHDELDKQC EQILGSLSDY
     TIIESVPFTS DAKTVATLWG IRKGMFPAVG AVREVGTTVI IEDVAFPVEN LANGVRDLQA
     LFDKYHYSEA IIFGHALEGN LHFVFTQGFE SQDEVTRYGG FMDDVAELVA VKYQGSLKAE
     HGTGRNMAPY VELEWGKDGY ALMQRIKKLF DPEGLLNPGV IINDSPTSHI ENLKPMPAAD
     DIVDRCIECG FCEPVCPSRT LTLSPRQRIV LYRELQRRRA QGENVEASEL EKVFEYQGLD
     TCAATGLCAD RCPVGINTGD LVKQLRTAKY QKFTPIAKWT ADHFSTTTSL TRASLKANQI
     AVKVLGENGV SKLVNGVRKL SHNKTPIWLP ETPQSNTHKL DNALELLVRS DKKVVYVPSC
     ASRTMGQQSD AQDQRSLTEV TLSLIKKAGF EVIIPDGIND QCCGMPYDSK GMTDIATAKS
     QQLEQALWKA SFEGEYPVLM DTSPCAKRSI ENFTQPLEIL EPTGFVSKYL LPHLDIVQKQ
     ETVMLHVTCS SRRMGLEGDM LKLAKACASD VILPEHIACC GWAGDKGFTT PELNAAAVHP
     LKEQVPNNCS RGFSNSRTCE IGLSHHSGIP YQSILYLVDE VSSAR
//