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Database: UniProt
Entry: A0A3D8IHN7_9HELI
LinkDB: A0A3D8IHN7_9HELI
Original site: A0A3D8IHN7_9HELI 
ID   A0A3D8IHN7_9HELI        Unreviewed;       942 AA.
AC   A0A3D8IHN7;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE            EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN   ORFNames=CQA53_07730 {ECO:0000313|EMBL:RDU64633.1};
OS   Helicobacter didelphidarum.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=2040648 {ECO:0000313|EMBL:RDU64633.1, ECO:0000313|Proteomes:UP000256379};
RN   [1] {ECO:0000313|EMBL:RDU64633.1, ECO:0000313|Proteomes:UP000256379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 17-337 {ECO:0000313|EMBL:RDU64633.1,
RC   ECO:0000313|Proteomes:UP000256379};
RA   Mannion A.J., Shen Z., Fox J.G.;
RT   "Novel Campyloabacter and Helicobacter Species and Strains.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:RDU64633.1}.
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DR   EMBL; NXLQ01000018; RDU64633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8IHN7; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000256379; 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   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; 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   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; PF12838; Fer4_7; 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   4: Predicted;
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:UP000256379}.
FT   DOMAIN          43..269
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          535..566
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          596..625
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   942 AA;  105346 MW;  32F09CDF17B948FC CRC64;
     MHKPSLLNKD YHAFYTEAKE FLENRIFIDY LHRFALGGDA SCYRYIPQIA IKAHNEDEII
     KILALSRKYQ LPLTFRAYGS SLSGQACSDS ILVITTFGWR DIEVSEKNIK LSCGVIGSEA
     NDALKAMGKK IGPDPATITM ASIGGIVSNN SSGMCCGVKQ NSYQTIESLR VILGDGTILD
     TSSKESVESF LATHADMAKS LLDLRSEILA DSELSTLIRR KYKIKNTTGY SLNALLDFDN
     ITDILNHLFV GAEGTLGFIS SVVLQNVDDE KYKACALLFY PDMNSTAYAI QILAQNDDII
     SSAEVMDYAS LKSVQGLEGL PSVIDEIHEG NACILIQTQS NDLSTLESNL VRIKDSLTHT
     NLLFPALYSQ DESEYSAWWK IRKGLLPIAS SLREDGSSVI TEDVCFEIEK FGEGVKFLQY
     LFEKYGFKDN GIIFGHALSG NVHFIITPNL NDAVQRENFE KLVEEMAQGV ANMGGSIKAE
     HGTGRMVAPF VEIEWGKKAY QINRKIKQIF DKANLINPDV IITDNPTIHT QNLKEMTKVD
     DFINKCMECG FCEKACPSNP LTLTPRQRIA VMREIQRLQN LGTQDAHELR DEMINEYVYV
     GDETCAACSM CATLCPLEID TAKIALHLRQ KQQKGLKVAN KILHNMNTTL HFAKFGLKMA
     SIFNPKFLHS ISSKFRAISP NLPYLPLNLP QANNYQFNDV VINTESSVVY FSTCINRAFA
     PSQNLSMNAD SRNIQEVFES ICKKAKVNVI YPQNLSNMCC GKAFVNYPTL QEENKQKIIR
     ELNIATNGGK IPIVLDHSAC SYHLIKLLMD SGLKIYDMPN YIYEVLHSKL QFHPKNENIA
     LYSMCALKKN NVSLEPLAKL CINGEIVIDR ALFCCGFAGN KGFFTPELNR NALQGFKRFY
     ANSKTRGISR GFGSSSTCEI GLNDNSEIYW QHIVYLVDEV TR
//
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