ID Q5V345_HALMA Unreviewed; 608 AA.
AC Q5V345;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN Name=sdhA1 {ECO:0000313|EMBL:AAV46057.1};
GN OrderedLocusNames=rrnAC1097 {ECO:0000313|EMBL:AAV46057.1};
GN ORFNames=E6P14_08075 {ECO:0000313|EMBL:QCP90821.1};
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569 {ECO:0000313|EMBL:AAV46057.1, ECO:0000313|Proteomes:UP000001169};
RN [1] {ECO:0000313|EMBL:AAV46057.1, ECO:0000313|Proteomes:UP000001169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:AAV46057.1}, and ATCC 43049 / DSM
RC 3752 / JCM 8966 / VKM B-1809 {ECO:0000313|Proteomes:UP000001169};
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2] {ECO:0000313|EMBL:QCP90821.1, ECO:0000313|Proteomes:UP000298722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:QCP90821.1,
RC ECO:0000313|Proteomes:UP000298722};
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) 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-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040}.
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DR EMBL; AY596297; AAV46057.1; -; Genomic_DNA.
DR EMBL; CP039138; QCP90821.1; -; Genomic_DNA.
DR RefSeq; WP_011223443.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V345; -.
DR STRING; 272569.rrnAC1097; -.
DR PaxDb; 272569-rrnAC1097; -.
DR EnsemblBacteria; AAV46057; AAV46057; rrnAC1097.
DR GeneID; 40152104; -.
DR KEGG; hma:rrnAC1097; -.
DR PATRIC; fig|272569.17.peg.1823; -.
DR eggNOG; arCOG00571; Archaea.
DR HOGENOM; CLU_014312_6_2_2; -.
DR Proteomes; UP000001169; Chromosome I.
DR Proteomes; UP000298722; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR Gene3D; 4.10.80.40; succinate dehydrogenase protein domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR003952; FRD_SDH_FAD_BS.
DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001169};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 5..387
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 479..608
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 608 AA; 66438 MW; 02BA0F3B30686FA6 CRC64;
MYEHDVIVVG AGGAGLRAAI AANEEGADVA LVTKLHPVRS HTGAAEGGIN AALQEGDSWD
LHAYDTMKGS DYLGDAPAID TFAKDAPEEV IQLEHWGMPF SREDDGRVSQ RPFGGLSYPR
TTYAGAETGH HLLHTMYEQA VKRGIEVYDE WYVTQLAVTD HDDPEDRVCH GCVAYDIKSG
EVQGFRANNG VILATGGLGQ AFDHTTNAVA NTGDGCAMAY RAGVPMEDME MIQFHPTTLP
STGVLISEGV RGEGGILYND NEERFMFEHG YANNEGELAS RDVVARAELT EVNEGRGVED
EYVDLDMRHL GEERILDRLE NILHLAEDFE GVDGLDEPMP VKPGQHYAMG GVETDENGET
CIDGLYAAGE TACVSLHGAN RLGGNALPEL LVFGARAGHH AAGKDMKTAE IQTGPSAKSE
PGDVEPPVDP GAIDASSGDV AADGAAIEPK AVLESTVEQE RQRIEDLIES DGINHAEVRA
DVQETMTDNV NVFRTEEGLE KALRDLRSAR KEYENVAVED PSRTYNTDLI HTIETRNILD
VAEAITLGAL AREEFRGAHW RAEHQERKDE EWIKHTMLAW NEGQPELYYK PVILEGDEET
YEPKVRSY
//