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Database: UniProt
Entry: T5CL49_HELPX
LinkDB: T5CL49_HELPX
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ID   T5CL49_HELPX            Unreviewed;       946 AA.
AC   T5CL49;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE            EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN   ORFNames=N404_05745 {ECO:0000313|EMBL:EQL53666.1};
OS   Helicobacter pylori FD506.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1191281 {ECO:0000313|EMBL:EQL53666.1, ECO:0000313|Proteomes:UP000015964};
RN   [1] {ECO:0000313|EMBL:EQL53666.1, ECO:0000313|Proteomes:UP000015964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD506 {ECO:0000313|EMBL:EQL53666.1,
RC   ECO:0000313|Proteomes:UP000015964};
RX   PubMed=23012278; DOI=10.1128/JB.01278-12;
RA   Gunaletchumy S.P., Teh X., Khosravi Y., Ramli N.S., Chua E.G., Kavitha T.,
RA   Mason J.N., Lee H.T., Alias H., Zaidan N.Z., Yassin N.B., Tay L.C.,
RA   Rudd S., Mitchell H.M., Kaakoush N.O., Loke M.F., Goh K.L., Vadivelu J.;
RT   "Draft genome sequences of Helicobacter pylori isolates from Malaysia,
RT   cultured from patients with functional dyspepsia and gastric cancer.";
RL   J. Bacteriol. 194:5695-5696(2012).
RN   [2] {ECO:0000313|EMBL:EQL53666.1, ECO:0000313|Proteomes:UP000015964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD506 {ECO:0000313|EMBL:EQL53666.1,
RC   ECO:0000313|Proteomes:UP000015964};
RX   PubMed=24051312;
RA   Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA   Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA   Loke M.F., Vadivelu J.;
RT   "Multiple genome sequences of Helicobacter pylori strains of diverse
RT   disease and antibiotic resistance backgrounds from malaysia.";
RL   Genome Announc. 1:E00687-E00713(2013).
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:EQL53666.1}.
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DR   EMBL; AKHO02000054; EQL53666.1; -; Genomic_DNA.
DR   RefSeq; WP_001157731.1; NZ_AKHO02000054.1.
DR   AlphaFoldDB; T5CL49; -.
DR   PATRIC; fig|1191281.5.peg.683; -.
DR   Proteomes; UP000015964; 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; 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}.
FT   DOMAIN          37..265
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          536..566
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   946 AA;  106001 MW;  66B3E898E2B6D5FB CRC64;
     MQENYDAFFT EASGFLNERV FKDYLRRLAY GIDASCYRYI PKIVAWVKDE EEVQKLCVLA
     KKHGVSLTFR AAGSSLSGQA SCDGVLVMAT HFFKDAKILN NATSIQLSCG VIGSNANALL
     KPYHKKIGPD PSTINTAMIG GIVANNASGM CCGVEQNSYK TLKSLRVILA DGILLDTANQ
     KSVEGFKNTH KDLIEGVLNL RKEILKDKEL HALIKKKYEI KNTTGYSLNA LIDFEDPIEI
     ISHLFIGSEG TLGFISSVEL ECVKDYAYKT CALLFYENLE QCAKAAQILA ALKAKQPETI
     SSAELMDYAC LKSVKGLEGM PRVILEIKEP NACLLIQSES DDPLILENNM QAILNALSAI
     PVVLDSQISS DPTIYQSWWK IRKGIFPIAA SQRRSQSSVI IEDVCFSQEN FVEGTKAIEG
     LLKKHDFKDN SIIFGHALSG NLHFVVTPIL ENETERKAFE NLVSDMFLMV SESFGSIKAE
     HGTGRMVAPF VEMEWGEKAY KIHKQIKELF DPNGILNPDV IITNDKEIHT KNLKSIHPIE
     EYLDMCMECG FCERVCPSKD LSLTPRQRIV IHREIEHLKE RVSQGHNEDQ ILLDELLKES
     EYLAHATCAV CHMCSMLCPL GIDTGKIALN YYQKNPKGEK IASKILNNMQ TTTSMARFSL
     KSARLVQNLI GSHNLVSLTK GIKKFIKPFP KAFNYMPKNN AYPLENKTHK SEEKVIYFST
     CINRSFAPST KMADKRCIQE VFESLCQKAK VSVMYPNGLN ALCCGKAFIN YTDLTKQNNE
     KNHEIFLQLS DNGKIPIVLD HSACSTHFFK QMKAYKDLKV YDLSVYIEEV LSPKLKFNPI
     NEDIGLYTMC ALKLENKEEL LLNLAKKCTL GEIVIHKETG CCGFAGNKGF FTPELNESAL
     SGFQAFYQSY DLKRGFSTSS TCEIGLSEKT HFSWQHIAYL VDACTL
//
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