ID A1S8D8_SHEAM Unreviewed; 935 AA.
AC A1S8D8;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN OrderedLocusNames=Sama_2440 {ECO:0000313|EMBL:ABM00645.1};
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297 {ECO:0000313|EMBL:ABM00645.1, ECO:0000313|Proteomes:UP000009175};
RN [1] {ECO:0000313|EMBL:ABM00645.1, ECO:0000313|Proteomes:UP000009175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) 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; CP000507; ABM00645.1; -; Genomic_DNA.
DR RefSeq; WP_011760551.1; NC_008700.1.
DR AlphaFoldDB; A1S8D8; -.
DR STRING; 326297.Sama_2440; -.
DR KEGG; saz:Sama_2440; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR eggNOG; COG1150; Bacteria.
DR HOGENOM; CLU_013688_0_0_6; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000009175; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009175}.
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 935 AA; 100877 MW; 507E107A4FA909EB CRC64;
MSVDYKAVIE ALKSRLGPQA VSDDPVRRFA WSTDASYFRI VPEVVVHADS LDEVQQTLAI
AREHGAPVTF RAAGTSLSGQ AIGPGILLML GHDGFRQLKV SSDGTKVSLG AAVIGADANA
ALKALDKKIG PDPATLASAM IGGIVNNNAS GMCCGTAQNS YQTIDSLRMV LADGTVLDTG
SEASRQAFEQ SHGALLNDLS NLAAMVKANH GLAARIRKKY AIKNTTGYSL NALVDFSCPF
DIINHLMVGS EGTLGFVEQV TYHTVDEARF KASAMAVFFS MEEAASAIPF LIGKSVAAAE
LLDWASIRAV TGKKGMPDWL SSLPEGAAIL LIESRAADAD TLQAYTEEVI GKIAHIPTER
PIVFSTDPAV YSKYWAMRSG LFPIIGGERP KGSSVIIEDV AFEVQHLAAA AKDLTALFHE
HGYPEGVIYG HALAGNFHFI ITPTFASQGD IDRFHGFMQA VAEMVINKYD GSMKAEHGTG
RAVAPFVEME WGSEAYTLMK SIKSLFDPSG LLNPGVILND DATVHVKNIK PCPVVDDLVD
KCIECGFCEK TCPTSALNLT PRQRIATLRE ISRLEASGDE EAASRMRDAA KYDVVDTCAA
CQLCTIACPV DNSMGQLVRK LRTPYISTTE QKVLDFQAKH FGAVNQVIST GFDTLGVIHK
LTGDTVTSAL MKVGRMVSKE VPYWDPSFPK GGALPKLPPH KVGQETLVYF PACGGRTFGP
TPLDKDKRPL PEVVVQVLER AGYNVVIPEH TRSLCCGQMW ESKGDFKNAD GKRRELIEAL
KAKSENGKLK VVVDALSCTK RTLGGDPDVE ILDLVEFLHD DVLSRLSIRQ KPLVTLHLGC
SARHLKVEAK MQAIADTCAK EVHKPAGIEC CGYAGEKGLY KPEINASALR NIKKLLPAAA
TEGYYANRMC EVGLSKHSGI SYRHLVYLLE ECSRG
//
