ID W0EA77_9FIRM Unreviewed; 901 AA.
AC W0EA77;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Heterodisulfide reductase {ECO:0000313|EMBL:AHF05966.1};
GN ORFNames=DESME_01885 {ECO:0000313|EMBL:AHF05966.1};
OS Desulfitobacterium metallireducens DSM 15288.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=871968 {ECO:0000313|EMBL:AHF05966.1, ECO:0000313|Proteomes:UP000010847};
RN [1] {ECO:0000313|EMBL:AHF05966.1, ECO:0000313|Proteomes:UP000010847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15288 {ECO:0000313|Proteomes:UP000010847};
RG DOE Joint Genome Institute;
RA Smidt H., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP007032; AHF05966.1; -; Genomic_DNA.
DR RefSeq; WP_006716419.1; NZ_CP007032.1.
DR AlphaFoldDB; W0EA77; -.
DR STRING; 871968.DESME_01885; -.
DR KEGG; dmt:DESME_01885; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_011400_0_0_9; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000010847; Chromosome.
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:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR004017; Cys_rich_dom.
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:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 1.
DR Pfam; PF02754; CCG; 2.
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; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000010847}.
FT DOMAIN 46..216
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 494..524
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 901 AA; 100589 MW; 1699C2720E566E26 CRC64;
MKNNLTTQQM EKLKMIFGDR VRFNKVERIV YSHDQGIMPD QIRSMIQCIP DGVVQPISAE
EVSLLAKAAH EEKIPLVPRG AGSAGFGGSV PAKGGIVVDF VRMNKINDIN IGHQTATVEP
GVIWSNLEKK LSEQGLTLRA YPSSSNSSTV AGWVAQGGSG YGSYEYGNCL QNIESVLMVF
PDGHLEKVEG SNLQQVYSLC GITGMIVEVT VKVHPKDEES VILAAFPDLP SASDFLNALN
NENVLLWNVS LTTPSYTALK QKALEHYVLP EDEYLITMVF PKPRRSIVEN KINKLVTRYN
GKIMRDKLAS EEWADKFYPM RFKKLGPTLV ASEVVIPIKE VAQFVREIER KFKGEFALEG
TMVGHDQISI LGFMLADERK LGFPMAYACS LDVIDAGEKH GGKVFSIGMY FTDRAKTFFG
EDRLKTIWNY KQFVDPDGLM NPGKIIPPSI DKQSPTKMLS ATMKFANAGC ELIGLAGRLL
SKWQTNNFSS PLDEQLTDDT FSCAMCGYCR NVCTVFDAVP WESNSPRGKY YILNQYIKGK
LPLDDEVGKA LYPCTTCKKC DAVCQIRAHN AHHWMNLRYE FDKHKLHNTG LEIIRNNVLT
TGNFWGVPAE ERLKWLDVPA QTHGKIAYWS GCWAGTIMDN MAQNATRILH QLNIPFVHFG
EKERCCGLYL SLGGYKKDFQ TLVKRNLEMF NEAGVETIIF SCPGCYATFN ENYPQMALEL
GIECNIRFKH IVVYLSELIA EGKIKFTEPF NHSVTYHDSC HVGRWFGHYD EPRNVLRSIP
GVELREMEHI KEQGLCCGLV SAFDSLPSVA HSGMKRVEEA VTTGAEYLVT NCAGCGSQFN
STCHAMGTQV QQMDLTELVA RALEIPTKDP SEKVGAYMAQ CVELLKDSVL APIVVPAETS
K
//
