ID O25820_HELPY Unreviewed; 948 AA.
AC O25820;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN OrderedLocusNames=HP_1222 {ECO:0000313|EMBL:AAD08264.1};
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962 {ECO:0000313|EMBL:AAD08264.1, ECO:0000313|Proteomes:UP000000429};
RN [1] {ECO:0000313|EMBL:AAD08264.1, ECO:0000313|Proteomes:UP000000429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695 {ECO:0000313|Proteomes:UP000000429};
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.P., Gill S., Dougherty B.A.,
RA Nelson K., Quackenbush J., Zhou L., Kirkness E.F., Peterson S., Loftus B.,
RA Richardson D., Dodson R., Khalak H.G., Glodek A., McKenney K.,
RA Fitzegerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D.,
RA Utterback T.R., Peterson J.D., Kelley J.M., Karp P.D., Smith H.O.,
RA Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD08264.1; -; Genomic_DNA.
DR PIR; F64672; F64672.
DR RefSeq; NP_208014.1; NC_000915.1.
DR AlphaFoldDB; O25820; -.
DR DIP; DIP-3097N; -.
DR IntAct; O25820; 4.
DR MINT; O25820; -.
DR STRING; 85962.HP_1222; -.
DR PaxDb; 85962-C694_06310; -.
DR EnsemblBacteria; AAD08264; AAD08264; HP_1222.
DR KEGG; hpy:HP_1222; -.
DR PATRIC; fig|85962.8.peg.1278; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR eggNOG; COG1150; Bacteria.
DR InParanoid; O25820; -.
DR OrthoDB; 9811557at2; -.
DR PhylomeDB; O25820; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IBA:GO_Central.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1903457; P:lactate catabolic process; IBA:GO_Central.
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 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:UP000000429}.
FT DOMAIN 39..267
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 539..568
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 948 AA; 106278 MW; 9E90D04719E1FE2F CRC64;
MRVEENYHAF FTEASGFLNE RIFKDYLRRL AYGIDASCYR YIPKIVAWVK NEEEVQKLCV
LAKKHGVSLT FRAAGSSLSG QAICDGVLVM VTHFFKDAQI LDNAQSIQLS CGVIGSNANA
LLKPYHKKIG PDPSTINTAM IGGIVANNAS GMCCGVEQNS YKTLKSLRVI LADGTLLDTA
NQESVESFKN AHKDLIEGVL NLRKEILEDK ELHALIKKKY EIKNTTGYSL NALIDFEDPI
EIISHLFIGS EGTLGFISSV ELECVKDYAY KTCALLFYEN LERCAKAAQI LAALKAKQPE
MISSAELMDY ACLKSVKGLE GMPSVVLEIK EPNACLLIQS ESDDPLILEN SMQTILNALS
AIPVVLDSQI SSDPSIYQSW WKIRKGIFPI AASKRKSQSS VIIEDICFSQ EDFVEGAKAI
EGLLKKHGFK DNGIIFGHAL SGNLHFVVTP ILENEAERKA FENLVSEMFL MVSKSSGSIK
AEHGTGRMVA PFVEMEWGEK AYKIHKQIKE LFDPNGILNP DVIITNDKEI HTKNLKSIYP
IEEHLDMCME CGFCERICPS KDLSLTPRQR IVIHREVEHL KERVSHGHHE DQVLLDELLK
ESEYLAHATC AVCHMCSTLC PLEIDTGKIA LNYYQKNPKG EKIASKILNH MQTTTSMARF
SLKSARLVQN LIGSHNLVSL TKGIKKFIKP FPKAFYYMPK NNAYPLENKT LKSEEKVIYF
STCINRSFAP SNKMADKRCI QEVFESLCQK AKVSVMYPNG LNALCCGKAF INYTDLTKQN
NEKNHAIFLQ LSDKGKIPIV LDHSACSTHF FKQMKAYKDL KVYDLSVYIE EVLSPKLKFN
PINEDIGLYT MCALKLENKE ELLFNLAKKC TLGEIVIHKE TGCCGFAGNK GFFTPELNES
ALNGFQAFYQ SYDLKRGFST SSTCEIGLSE KTRFSWQHIA YLVDACTL
//
