ID I9NZG5_9ALTE Unreviewed; 919 AA.
AC I9NZG5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=AGRI_15035 {ECO:0000313|EMBL:EIW87844.1};
OS Alishewanella agri BL06.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alishewanella.
OX NCBI_TaxID=1195246 {ECO:0000313|EMBL:EIW87844.1, ECO:0000313|Proteomes:UP000035062};
RN [1] {ECO:0000313|EMBL:EIW87844.1, ECO:0000313|Proteomes:UP000035062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL06 {ECO:0000313|EMBL:EIW87844.1,
RC ECO:0000313|Proteomes:UP000035062};
RX PubMed=22933763; DOI=10.1128/JB.01129-12;
RA Kim J., Jung J., Sung J.S., Chun J., Park W.;
RT "Genome Sequence of Pectin-Degrading Alishewanella agri, Isolated from
RT Landfill Soil.";
RL J. Bacteriol. 194:5135-5136(2012).
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:EIW87844.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKKU01000026; EIW87844.1; -; Genomic_DNA.
DR RefSeq; WP_008985750.1; NZ_AKKU01000026.1.
DR AlphaFoldDB; I9NZG5; -.
DR STRING; 1195246.AGRI_15035; -.
DR PATRIC; fig|1195246.3.peg.2984; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR eggNOG; COG0479; Bacteria.
DR Proteomes; UP000035062; 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; 3.30.70.2740; -; 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; 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:UP000035062}.
FT DOMAIN 35..263
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 527..558
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 586..615
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 919 AA; 100423 MW; 2791F1B10D4EC0AC CRC64;
MQPQFLHAVQ QLIPAERYFD DPLSTLAFGT DASFYRLTPK LVLRVESEQE VIALLKLAGQ
YQVPLTFRAA GTSLSGQAVT DSVLLVLGEN WQQYQIFELG ERIRLAPGVI GAQANQWLAP
YGRKIGPDPA SINSCKIGGI VANNASGMCC GTAQNSFNTL HGMRLVLADG TVLDTEDAAS
VAAFRQSHAP LLAELSTLAQ QTCDNPELLA KIRHKYRLKN TMGFSLNALT EFSDPIDILS
HLMVGSEGCL GFISSVTYQT VPEHPHKASA LYVFPDIASC CQAVTLLKDT PVAAVELLDR
RSLRSVQHKA GLPAWVATLS EGAAALLIES RAATVPQLER QIATIQQQLA AFELEQKVEF
TREPAVCEQL WAIRKGTFPA VGAVRETGTT VIIEDVTFPL PRLAEGVLAL QRLFDRFGYH
EAIIFGHALE GNLHFVFTQS FNSATEIQRY ADFMREVAQL VAVEFGGALK AEHGTGRNMA
PFVELEWGTE AYQLMWRIKQ LLDPQHILNP EVVLSRDSQL HLKHLKALPA ADPLVDKCIE
CGFCEPVCPS RKLTLTPRQR IVAQREISLL QQSGEDSARL AALQQAYQYA GTDTCAACGL
CSTACPVGIN TGDLTRQLRG RANQRFQGLA NFAASKFSVI SSLGRTALNI GQLGARMLGP
AMPLWHQAMP TAARAFQLPD QPDLDSGLIP VLYFGSCSGR VMGPQQHSQD LRSLAEVSAN
LLQKAGYQLF QPPKLAQQCC GMPFQSKGQF AAAKQLQQQL HQWLMQHSEQ GRIAVFCDSS
PCSLTLREAL DPRLQLFDSI DFIYDKVLPK LKLNKQAAPL ALHISCSAQQ LEQGRKLTEL
AAACTEQLVI PEGISCCGFA GDKGFFLPEL NASALSDLAR QVSKCSRGVS SSRTCEIGLS
RHSGVEYQHL LYLLDAQSD
//
