ID A0A0F5VGW0_9GAMM Unreviewed; 938 AA.
AC A0A0F5VGW0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=KY46_06375 {ECO:0000313|EMBL:KKD00720.1};
OS Photobacterium halotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=265726 {ECO:0000313|EMBL:KKD00720.1, ECO:0000313|Proteomes:UP000033633};
RN [1] {ECO:0000313|EMBL:KKD00720.1, ECO:0000313|Proteomes:UP000033633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MELD1 {ECO:0000313|EMBL:KKD00720.1,
RC ECO:0000313|Proteomes:UP000033633};
RA Mathew D.C., Huang C.-C.;
RT "Mercury Reductase activity and rhizosphere competence traits in the genome
RT of root associated Photobacterium halotolerans MELD1.";
RL Submitted (DEC-2014) 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:KKD00720.1}.
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DR EMBL; JWYV01000003; KKD00720.1; -; Genomic_DNA.
DR RefSeq; WP_046219789.1; NZ_JWYV01000003.1.
DR AlphaFoldDB; A0A0F5VGW0; -.
DR STRING; 265726.KY46_06375; -.
DR PATRIC; fig|265726.11.peg.3180; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000033633; 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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000033633}.
FT DOMAIN 38..266
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 530..561
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 938 AA; 102961 MW; E34740550A248BB6 CRC64;
MTDNYQQLIQ QLGTFLDAGQ IITDEARRLA YGTDASFYRL IPRVVLRLHN QHQVIAVIRA
CAELNIPHTY RAAGTSLSGQ AVSDSVLITL SDQWRRHIIE DNGLKITLQP GVIGADANRY
LAPYGRKIGP DPASINTCKI GGIAANNASG MCCGTAQNSY RTVDGMTVIL TDGTVLNTRD
EASKAAFRRS HASLLSDLTE LRKEVDTNPA LKDKIQHKYR LKNTTGYALN ALTDFSDPID
ILEHLMIGSE GTLGFIADIT YKTVIEHPHK ASSLLVFSTI EQASEATSIL ATTPVSAVEM
MDGRAMRSVA DKAGMPEFIA HLDLEAAALL VETRAGTHEE LLSQCDAIMA SLSAFTVIAS
VPFTSEPATV NTLWAIRKGM FPAVGAVRET GTTVIIEDVA FPVANLAQGV RDLQALFAQF
GYHEAIIFGH ALEGNLHFVF TQGFDVQSEI DRYGAFMDAV AELVAVKYQG SLKAEHGTGR
NMAPYVELEW GKAGYQLMQR IKRLFDPQGL LNPGVIINDD PHAHLRHLKP MPAADDLVDR
CIECGFCEPV CPSRTLSLSP RQRIVLYREL QHRRRNGDTA GAKALDTVFQ YQGIDTCAAT
GLCAERCPVG INTGDLIKKL RTDKYQRFLP IARWTADHFA TTTRLIKTGL GVAHSAQSLL
GEHRMTALSN TARRWSHNST PQWLPELPTI NRHQLTESGN SQAHGEKKVV YLPTCASRTM
GQQPDNPDQR PLTEVTLSLI AKAGFDVVIP QGLNDLCCGM PYDSKGMTEP AAQKSQQLEE
TLWQASEQGK YPILIDASPC AKRSVESFSR LMNIVEPVGL VLHYLLPYLE LKRLHETVML
HVTCSSRKMG LENDMLELAK ACASTVIVPE HIQCCGWAGD KGFSVPELNA VSLEPLKDQV
PPDCRRGFSN SRTCEIGLSH HSGVPYQSIL YLVDEVAR
//
