ID L0KCW6_HALHC Unreviewed; 809 AA.
AC L0KCW6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=NAD(FAD)-dependent dehydrogenase {ECO:0000313|EMBL:AGB42229.1};
GN OrderedLocusNames=Halha_2355 {ECO:0000313|EMBL:AGB42229.1};
OS Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Halobacteroides.
OX NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB42229.1, ECO:0000313|Proteomes:UP000010880};
RN [1] {ECO:0000313|Proteomes:UP000010880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35273 / DSM 5150 / MD-1
RC {ECO:0000313|Proteomes:UP000010880};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Gu W.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Halobacteroides halobius DSM 5150.";
RL Submitted (FEB-2012) 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 sulfur carrier protein TusA family.
CC {ECO:0000256|ARBA:ARBA00008984}.
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DR EMBL; CP003359; AGB42229.1; -; Genomic_DNA.
DR AlphaFoldDB; L0KCW6; -.
DR STRING; 748449.Halha_2355; -.
DR KEGG; hhl:Halha_2355; -.
DR PATRIC; fig|748449.3.peg.2275; -.
DR eggNOG; COG0425; Bacteria.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR eggNOG; COG2210; Bacteria.
DR HOGENOM; CLU_003291_3_1_9; -.
DR Proteomes; UP000010880; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd01524; RHOD_Pyr_redox; 1.
DR Gene3D; 3.40.1260.10; DsrEFH-like; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR Gene3D; 3.30.110.40; TusA-like domain; 1.
DR InterPro; IPR032836; DsrE2-like.
DR InterPro; IPR027396; DsrEFH-like.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001455; TusA-like.
DR InterPro; IPR036868; TusA-like_sf.
DR PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 1.
DR Pfam; PF13686; DrsE_2; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF01206; TusA; 1.
DR PRINTS; PR00368; FADPNR.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF75169; DsrEFH-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF64307; SirA-like; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS01148; UPF0033; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000010880}.
FT DOMAIN 442..530
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 529..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 809 AA; 88275 MW; 823A1C71D68B7A89 CRC64;
MDEEAEIVIF EKGAHISFAN CGLPYHIGEV IEEREKLLVQ TPEAMKARFD IDVRVKNEVL
KIDREAEELE IKDLNSNETY RESYDYVVLS PGADPIKPPL PGMDGEKIFT LRNIPDTDQI
KGFVDNNNPQ HAVVVGAGYI GVEMAENLHE RGLDVSVVEM APQVLGPIDR EMAAQVHNHL
RMKGIELYLD NGVAGFADQD KRKKVELQDG TELTTDLVIM SAGVSPNTKL AEEAGLEIGQ
TRAIKVNDYL QTSDEKIYAI GDAIEVTDVI TGQPAHIPLA GPANKQGRIV ANNLVGDKEK
FKGSQGTAIA KVFDLEVGAT GNNEKQLQAA GIDYQVSYIN KKNHAGYYPG AVPLMLKILF
TPKDGKLLGA QAIGYDGVDK RIDVLATAIR FEKTVFDLQD IDLAYAPPFG SAKDPVNMAG
FTAGNILTGK MDVIQWHEIA DLDSETIILD VREEIEVQLG KIDNSVNIPL NQLRDRLDEL
DSDKEIVVYC AVGLRGYIAT RILLQNGFNN VKNLAGGYKL YSAVQKDQNE VVDDSTTPNQ
DKLASISNPE EGQQAEEEIE MATSEGERVK LDACGLQCPG PIMQVSKKLQ ELNDGDILEV
VATDPGFTAD IKAWCQSTGN TLLTTGNQGS EFTAEIKKGQ SDQPLGNNQS APAKNGATMV
VFEGSLDKAI ASFIIANGAA SMGKDVTLFF TFWGLNVLRK NQDIDVDKGL MDQMFGKMMP
QGSKELPLSN MNMFGMGPKM IRNVMENKGV DSLESLMKQA QENGVRLVAC QMTMDMLGIQ
KEELIDGVEV GGVATFLNSA DQSNMSLFI
//
