ID B2RI21_PORG3 Unreviewed; 647 AA.
AC B2RI21;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Fumarate reductase flavoprotein subunit {ECO:0000313|EMBL:BAG33016.1};
GN OrderedLocusNames=PGN_0497 {ECO:0000313|EMBL:BAG33016.1};
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947 {ECO:0000313|EMBL:BAG33016.1, ECO:0000313|Proteomes:UP000008842};
RN [1] {ECO:0000313|EMBL:BAG33016.1, ECO:0000313|Proteomes:UP000008842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
RC 2561 {ECO:0000313|Proteomes:UP000008842};
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
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DR EMBL; AP009380; BAG33016.1; -; Genomic_DNA.
DR RefSeq; WP_004584032.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RI21; -.
DR SMR; B2RI21; -.
DR GeneID; 29255729; -.
DR KEGG; pgn:PGN_0497; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_7_0_10; -.
DR OrthoDB; 9806724at2; -.
DR BioCyc; PGIN431947:G1G2V-545-MONOMER; -.
DR Proteomes; UP000008842; Chromosome.
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; 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; 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; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR01811; sdhA_Bsu; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF53; SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PRINTS; PR00368; FADPNR.
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.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 36..449
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 511..645
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 338
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ SEQUENCE 647 AA; 72365 MW; 3BF0D7B89AB00BE9 CRC64;
MATINSKIPA GPLKDKWTNY KDHQKLVNPA NKRRLDIIVV GTGLAGASAA ASFGEMGFNV
LNFCIQDSPR RAHSIAAQGG INAAKNYQND GDSVYRLFYD TIKGGDYRAR EANVYRLAEV
SNAIIDQCVA QGVPFAREYG GLLDNRSFGG AQVSRTFYAR GQTGQQLLLG AYSALSRQVG
LGKVKLYTRY EMLDVVLIDG RARGILARNL VTGKIERFAA HAVVIATGGY GNAFFLSTNA
MASNGSAAWQ CYKKGAFFAN PCMAQIHPTC IPVHGDYQSK LTLMSESLRN DGRIWVPKDI
EDAGRLQRGE IKGKDIPEEK RDYYLERRYP AFGNLVPRDV ASRAAKERCD AGYGVNNTGL
AVFLDFGDAI KRLGRDVVEQ KYGNLFQMYE KIADENPYET PMMIYPAIHY TMGGLWVDYE
LMTTIPGLFA IGEANFSDHG ANRLGASALM QGLADGYFVI PYTMQNYLAD QIQVPRFSTD
RPEFEAAEKE LQDRITRIMN VKGNKSVDDL HKELGHIMWD NVGMGRDKAG LEKAIVKLDE
LKKEFWSNVY VPGEANDLNV ELEKALRLAD FIEIGTLMAH DAMDREESCG GHFRIEHQTE
EGEAKRDDEN FAYVSCWEYQ GEDKDPIMYK EELVYEETVR AQRNYKS
//
