ID B0TQ40_SHEHH Unreviewed; 939 AA.
AC B0TQ40;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN OrderedLocusNames=Shal_3084 {ECO:0000313|EMBL:ABZ77632.1};
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817 {ECO:0000313|EMBL:ABZ77632.1, ECO:0000313|Proteomes:UP000001317};
RN [1] {ECO:0000313|EMBL:ABZ77632.1, ECO:0000313|Proteomes:UP000001317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4 {ECO:0000313|EMBL:ABZ77632.1,
RC ECO:0000313|Proteomes:UP000001317};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-2008) 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; CP000931; ABZ77632.1; -; Genomic_DNA.
DR RefSeq; WP_012278158.1; NC_010334.1.
DR AlphaFoldDB; B0TQ40; -.
DR STRING; 458817.Shal_3084; -.
DR KEGG; shl:Shal_3084; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR eggNOG; COG1150; Bacteria.
DR HOGENOM; CLU_013688_0_0_6; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000001317; Chromosome.
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}.
FT DOMAIN 38..267
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 531..562
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 588..620
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 939 AA; 102366 MW; AC8C5C4072316ADB CRC64;
MSINYEAILR DLRRQVGEHA ATNDPVRRFA WSTDASYFRI VPEIVVHADT LEQAKRTLAI
ARTYGAPVTF RAAGTSLSGQ AIGEGILLIL GHDGFRTLIV SEDASKITLG TAVIGADANA
ALKPLNKKIG PDPATLAAAK IGGIVSNNAS GMCCGTAQNS YQTIASAKLL FADGTELDTG
CEESKAAFTQ SHPQLLKQLT ELAELTVNNT TLAARIRKKY SIKNTTGYSL NALVDFADPF
ELINHLIVGA EGTLAFVEEV TYHTVDEARF KASAMAVFFN MEDAARAIPP LVGDSVAAAE
LLDWASIKAV TGKAGMPEWL AQLPEGASIL LIESRANDKD TLERYTKDVT AKLAHIETER
PIIFSDDPAV FGQYWAMRSA LFPIIGGERP KGTSVIIEDV AFELEHLAAA ANDLTELFHK
HNYPEGVIYG HALAGNFHFI ITPTFNSQID IERFHAFMQD VAEMVINKYD GSMKAEHGTG
RAVAPFVEME WGSDAYSLMK RIKQIFDPEG LLNPGVILND DNQIHVKNIK PCPVVDDLID
KCIECGFCEK TCPTSALNMS PRQRIATLRE IERLEQSGGK RAAEQMRAAA KYDVVDTCAA
CQLCTIACPV DNSMGELVRK LRTPYITSTE QKVLDFQAKH FGAVNQVIST GFDVLGTIHK
ITGSAVTGAI MKAGRVISKE VPYWNPDFPK GGKLPKLAAP IPGQETVVYF PACGGRTFGP
TPKDPDNRTL PEVVVTLLER SGYNVITPEK TRDLCCGQMW ESKGDFKNAD AKRKELIEVV
AAMTQGGKLP VIIDALSCTY RTLAGDKSLS DKVEIVDMVD FIHDKLLDKL TITRKKPAVA
LHLGCSARKM KVEPKMEAIV DACSNRVVRP AGINCCGYAG EKGLYKPEIN ASALRNIKKL
IPVDVSEGYY ANRMCEVGLT QHSGISYRHL AYLLEECTR
//
